Nanoparticle compositions associated with celastrol and / or rapamycin

Abstract

The present invention relates to compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol and / or rapamycin. In particular, the present invention relates to nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, and related methods of use (e.g., in diagnostic and / or therapeutic settings), and optionally, a plurality of tolerogenic antigens.

Description

[0001]UM-43148.601 NANOPARTICLE COMPOSITIONS ASSOCIATED WITH CELASTROL AND / OR RAPAMYCIN CROSS-REFERENCE TO RELATED APPLICATION The present application claims priority to U.S. Provisional Application No.63 / 647,302, filed May 14, 2024, which is incorporated herein by reference in its entirety. SEQUENCE LISTING The text of the computer readable sequence listing filed herewith, titled “UM_43148_601_SequenceListing.xml”, created May 13, 2025, having a file size of 512,635 bytes, is hereby incorporated by reference in its entirety. FIELD OF THE INVENTION The present invention relates to compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol and / or rapamycin. In particular, the present invention relates to nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, and related methods of use (e.g., in diagnostic and / or therapeutic settings), and optionally, a plurality of tolerogenic antigens. BACKGROUND OF THE INVENTION Celastrol and rapamycin are each demonstrated effective therapeutics for a variety of disorders and conditions. Despite their huge potential, therapeutic delivery of such drugs is at times challenging, partially due to lack of effective drug delivery platforms. As such, improved compositions and techniques for stable and targeted delivery (e.g., in vitro or in vivo) of celastrol and / or rapamycin are needed. SUMMARY OF THE INVENTION Experiments conducted during the course of developing embodiments for the present invention resulted in the formulation and characterization of Celastrol-DMPC sHDL nanoparticles and Celastrol-DPPC sHDL nanoparticles. Such experiments further quantified Celastrol loading in DMPC sHDL nanoparticles via UV-VIS spectroscopy. In addition, such experiments demonstrate the effects of Celastrol on RAW 264.7 macrophage cell line stimulation response, and inhibition of NF-κB activation by Celastrol in THP-1 NF-κB reporter cell line and cytotoxicity assessment. The effects of Celastrol-DMPC sHDL nanoparticles on UM-43148.601 inflammatory responses in human fibroblast-like synoviocytes (FLS) were additionally demonstrated in such experiments. Accordingly, the present invention relates to compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol and / or rapamycin. In particular, the present invention relates to nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, and related methods of use (e.g., in diagnostic and / or therapeutic settings), and optionally, a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle associated with celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises a mixture of at least one phospholipid and at least one HDL apolipoprotein or apolipoprotein mimetic, wherein the sHDL nanoparticle is optionally further associated with a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), at least one phospholipid selected from 1,2-dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC), at least one HDL apolipoprotein or apolipoprotein mimetic, and optionally a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or variant thereof) and / or rapamycin (or a variant thereof), at least one phospholipid selected from 1,2-dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC) and at least one HDL apolipoprotein or apolipoprotein mimetic, and a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises at least one phospholipid selected from 1,2- dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC), at least one HDL apolipoprotein or apolipoprotein mimetic, and optionally a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises at least one phospholipid selected from 1,2- dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC) UM-43148.601 and at least one HDL apolipoprotein or apolipoprotein mimetic, and a plurality of tolerogenic antigens. In some embodiments, the phospholipid is selected from the group consisting of 1,2- dilauroyl-sn-glycero-3-phosphocholine; 1,2-dimyristoyl-sn-glycero-3-phosphocholine; 1,2- dipalmitoyl-sn-glycero-3-phosphocholine; 1,2-distearoyl-sn-glycero-3-phosphocholine; 1,2- diarachidoyl-sn-glycero-3-phosphocholine; 1,2-dibehenoyl-sn-glycero-3-phosphocholine; 1,2- dilignoceroyl-sn-glycero-3-phosphocholine; 1,2-dimyristoleoyl-sn-glycero-3-phosphocholine; 1,2-dimyristelaidoyl-sn-glycero-3-phosphocholine; 1,2-dipalmitoleoyl-sn-glycero-3- phosphocholine; 1,2-dipalmitelaidoyl-sn-glycero-3-phosphocholine; 1,2-dipetroselenoyl-sn- glycero-3-phosphocholine; 1,2-dioleoyl-sn-glycero-3-phosphocholine; 1,2-dielaidoyl-sn- glycero-3-phosphocholine; 1,2-dieicosenoyl-sn-glycero-3-phosphocholine; 1,2-dinervonoyl-sn- glycero-3-phosphocholine; 1,2-dilauroyl-sn-glycero-3-phosphoethanolamine; 1,2-dimyristoyl- sn-glycero-3-phosphoethanolamine; 1,2-dipentadecanoyl-sn-glycero-3-phosphoethanolamine; 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine; 1,2-distearoyl-sn-glycero-3- phosphoethanolamine; 1,2-dipalmitoleoyl-sn-glycero-3-phosphoethanolamine; 1,2-dielaidoyl- sn-glycero-3-phosphoethanolamine; 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine; dioleoyl- sn-glycero-3-phosphoethanolamine-N-[3-(2-pyridyldithio) propionate]; 1,2-dipalmitoyl-sn- glycero-3-phosphothioethanol; 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine-N- [4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine- N-[4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn-glycero-3- phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]; 1,2-di-(9Z- octadecenoyl)-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane- carboxamide]; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Distearoyl; N-[(3-Maleimide-1- oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N- (3-Maleimide-1-oxopropyl)-L-α-phosphatidylethanolamine, Dimyristoy; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Dioleoyl; N-(3-Maleimide-1-oxopropyl)-L-α- phosphatidylethanolamine, Dipalmitoyl; N-(3-Maleimide-1-oxopropyl)-L-α- phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; phosphatidylcholine; phosphatidylinositol; phosphatidylserine; phosphatidylethanolamine; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Distearoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dioleoyl; N-(Succinimidyloxy-glutaryl)-L-α- UM-43148.601 phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dipalmitoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dimyristoyl; 3-(N-succinimidyloxyglutaryl)aminopropyl, and polyethyleneglycol-carbamyl distearoylphosphatidyl-ethanolamine; N-(3-oxopropoxy polyethyleneglycol)carbamyl-distearoyl-ethanolamine. In some embodiments, the HDL apolipoprotein component is selected from the group consisting of apolipoprotein A-I (apoA-I), apolipoprotein A-II (apoA-II), apolipoprotein A-II xxx (apoA-II-xxx), apolipoprotein A4 (apoA4), apolipoprotein Cs (apoCs), apolipoprotein E (apoE), apolipoprotein A-I milano (apoA-I-milano), apolipoprotein A-I paris (apoA-I-paris), apolipoprotein M (apoM), an HDL apolipoprotein mimetic, preproapoliprotein, preproApoA-I, proApoA I, preproApoA-II, proApoA II, preproApoA-IV, proApoA-IV, ApoA-V, preproApoE, proApoE, preproApoA IMilano, proApoA-IMilano, preproApoA-IParis, proApoA-IParis, and mixtures thereof. In some embodiments, the apolipoprotein mimetic is described by any of SEQ ID NOs: 1-336 and WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341), LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358), LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), UM-43148.601 PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373). In some embodiments, the plurality of tolerogenic antigens are tolerogenic antigens comprising between 3 amino acids and 50 amino acids in length. In some embodiments, the plurality of tolerogenic antigens are tolerogenic antigens comprising a polypeptide comprising a nucleic acid sequence of any one of SEQ ID NOs: 375-796. In some embodiments, the plurality of tolerogenic antigens are human allograft transplantation antigens. In some embodiments, the human allograft transplantation antigens are selected from subunits of the various MHC class I and MHC class II haplotype proteins, and single-amino-acid polymorphisms on minor blood group antigens including RhCE, Kell, Kidd, Duffy and Ss. In some embodiments, the plurality of tolerogenic antigens are specific for type 1 diabetes mellitus. In some embodiments, the plurality of tolerogenic antigens are selected from insulin, proinsulin, pre-proinsulin, glutamic acid decarboxylase-65 (GAD-65), GAD-67, insulinoma-associated protein 2 (IA-2), insulinoma-associated protein 213 (IA-213), ICA69, ICA12 (SOX-13), carboxypeptidase H, Imogen 38, GLIMA 38, chromogranin-A, HSP-60, caboxypeptidase E, peripherin, glucose transporter 2, hepatocarcinoma-intestine- pancreas / pancreatic associated protein, S10013, glial fibrillary acidic protein, regenerating gene II, pancreatic duodenal homeobox 1, dystrophia myotonica kinase, islet-specific glucose-6- phosphatase catalytic subunit-related protein, and SST G-protein coupled receptors 1-5. In some embodiments, the plurality of tolerogenic antigens are specific for one or more of the following autoimmune disorders: rheumatoid arthritis, multiple sclerosis, diabetes, autoimmune diseases of the thyroid, thyroid-associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutieres syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), UM-43148.601 Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease. In some embodiments, the plurality of tolerogenic antigens comprises one or more of tolerogenic antigens selected from thyroglobulin (TG), thyroid peroxidase (TPO), thyrotropin receptor (TSHR), sodium iodine symporter (NIS), megalin, thyroid autoantigens including TSHR, insulin-like growth factor 1 receptor, calcium sensitive receptor, 21-hydroxylase, 17a- hydroxylase, and P450 side chain cleavage enzyme (P450scc), ACTH receptor, P450c21, P450c17, FSH receptor, a-enolase, pituitary gland-specific protein factor (PGSF) 1 a and 2, and type 2 iodothyronine deiodinase, myelin basic protein, myelin oligodendrocyte glycoprotein, proteolipid protein, collagen II, W, K+-ATPase, tissue transglutaminase and gliadin, tyrosinase, tyrosinase related protein 1 and 2, acetylcholine receptor, desmoglein 3, 1 and 4, pemphaxin, desmocollins, plakoglobin, perplakin, desmoplakins, acetylcholine receptor, BP180, BP230, plectin, laminin 5, endomysium, tissue transglutaminase, collagen VII, matrix metalloproteinase 1 and 3, the collagen-specific molecular chaperone heat-shock protein 47, fibrillin-1, PDGF receptor, Scl-70, U1 RNP, Th / To, Ku, Jo 1, NAG-2, centromere proteins, topoisomerase I, nucleolar proteins, RNA polymerase I, II and Ill, PM-Sic, fibrillarin, 823, U1snRNP, nuclear antigens SS-A and SS-8, fodrin, poly(ADP-ribose) polymerase, topoisomerase, nuclear proteins including SS-A, high mobility group box 1 (HMGB1), nucleosomes, histone proteins, double- stranded DNA, glomerular basement membrane proteins including collagen IV, cardiac myosin, aromatic L-amino acid decarboxylase, histidine decarboxylase, cysteine sulfinic acid decarboxylase, tryptophan hydroxylase, tyrosine hydroxylase, phenylalanine hydroxylase, hepatic P450 cytochromes P4501A2 and 2A6, SOX-9, SOX-10, calcium-sensing receptor protein, and type 1 interferons interferon alpha, beta and omega. In some embodiments, the plurality of tolerogenic antigens are specific for celiac disease. In some embodiments, the plurality of tolerogenic antigens are selected from gliadin, glutenin, and fragments thereof capable of inducing an immune response. In some embodiments, the plurality of tolerogenic antigens are conjugated to the outer surface of the sHDL nanoparticle. In some embodiments, the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid. In some embodiments, the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid via a linker. In some embodiments, the linker is selected from non-ester containing linker moieties and ester-containing linker moieties. In some embodiments, the celastrol (or a UM-43148.601 variant thereof) and / or rapamycin (or a variant thereof) is non-covalently attached to the phospholipid. In some embodiments, the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is admixed with the sHDL. In some embodiments, the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is adsorbed onto or into the sHDL. In some embodiments, the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is encapsulated within the sHDL. In some embodiments, the average particle size of the sHDL nanoparticle is between 6 to 500 nm. In certain embodiments, the present invention provides a method for treating and / or preventing a condition, disorder, and / or disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In some embodiments, the condition, disorder, and / or disease is selected from erythropoietic porphyries, T2 diabetes, antifibrinolytic, central diabetes insipidus, delaying the birth in case of threat of premature birth, antibiotic, cystic fibrosis, angina, anticoagulant in patients with unstable angina undergoing PTCA or PCI, systemic lupus erythematosus, hypercalcemia, osteoporosis, pagets disease, carbetocin works as an oxytocic, antihemorrhagic and uterotonic drug in the peripheral nervous system, prevention of uterine atony, induction, and control postpartum bleeding or haemorrhage, stimulant of the gastric secretion, for treat hormone-sensitive cancers of the prostate and breast, inhibition of premature LH surges in women undergoing controlled ovarian stimulation, immunosuppression in organ transplantation to prevent rejection, peritumoral brain edema, diagnosis of ACTHdependent Cushing’s syndrome, allergies, ankylosing spondylitis, psoriasis, chorioditis, erythema, keratitis, sclerosis, dermatomyositis, rheumatoid arthritis, Stevens-Johnson Syndrome, ulcerative colitis, diagnosis of adrenocortical insufficiency, antibiotic, systemic infections caused by gram positive organisms, nocturnal enuresis, nocturia, and stoppage of bleeding or haemorrhage in haemophilia A patients, acute hereditary angioderma, postmenopausal osteoporosis, anti- parathyroid, Paget’s disease, hypercalcaemia, hypertension, AIDS / HIV-1 infection, acute coronary syndrome, unstable angina undergoing PCI, Alzheimer’s and Parkinson’s disease, inhibition of premature LH surges in women undergoing controlled ovarian hyperstimulation, Relapsing- Remitting Multiple Sclerosis, hepatic insufficiency, wound healing, inflammation of respiratory tract, asthenia, release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary, stimulate the secretion of gonadotropin during disturbances fertility, and diagnosis of the functional capacity and response of the gonadotropes UM-43148.601 of the anterior pituitary, for skin lesions, surface wounds and eye infections, postmenopausal osteoporosis, Paget’s disease, hypercalcaemia, hereditary angioedema, immune system related diseases, acromegaly, anticoagulant, fibroids and endometriosis, central diabetes insipidus, Cushing’s syndrome, diabetic foot ulcers, treatment of central precocious puberty, uterine fibriods and endometriosis, vasodilatory, natriuretic, diuretic and neurohormonal effects, acromegaly, carcinoid syndrome, acute bacterial skin and skin structure infections, initiation or improvement of uterine contractions, and control postpartum bleeding or haemorrhage, hematide Chronic kidney disease associated anemia, stomatitis, pharyngitis, diagnostic assessment of thyroid function, postmenopausal osteoporosis, hypercalcaemia, diagnosis of pancreatic exocrine dysfunction, and gastrinoma, Zollinger-Ellison syndrome, prevention of RDS in premature infants, and meconium aspiration syndrome, acute variceal bleeding, allergic rhinitis and conjunctivitis, spinocerebellar degeneration / ataxia, Short Bowel Syndrome, antibiotic, bactericidal, teriparatide is the only anabolic (i.e., bone growing) agent indicated for use in postmenopausal women with osteoporosis, Cortrosyn Analogue of adrenocorticotrophic hormone (ACTH) used for diagnostic purposes, treatment of adrenal insufficiency, epilepsia, Chronic hepatitis B, chronic hepatitis C, primary and secondary immune deficiencies, acute decompensated heart failure, colitis, esophageal variceal bleeding in patients with cirrhotic liver disease and AIDS-related diarrhea, sarcoidosis and acute lung injury, and severe chronic pain. In certain embodiments, the present invention provides a method for treating and / or preventing arthritis and / or rheumatoid arthritis in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing eczema in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing tuberculosis in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing obesity in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing Crohn’s disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. UM-43148.601 In certain embodiments, the present invention provides a method for treating and / or preventing prostate cancer in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing organ transplant rejection in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing an autoimmune disorder in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In some embodiments, the autoimmune disorder is selected from multiple sclerosis (MS), celiac disease, rheumatoid arthritis, diabetes (e.g., type 1 diabetes mellitus), autoimmune diseases of the thyroid (e.g., Hashimoto's thyroiditis, Graves' disease), thyroid- associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutières syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease. In certain embodiments, the present invention provides a method for treating and / or preventing an inflammatory disorder in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In some embodiments, the inflammatory disorder is selected from idiopathic inflammatory diseases or disorders, chronic inflammatory diseases or disorders, acute inflammatory diseases or disorders, autoimmune diseases or disorders, infectious diseases or disorders, inflammatory malignant diseases or disorders, inflammatory transplantation-related diseases or disorders, inflammatory degenerative diseases or disorders, diseases or disorders associated with a hypersensitivity, inflammatory cardiovascular diseases or disorders (e.g., as described herein), inflammatory cerebrovascular diseases or disorders, peripheral vascular diseases or disorders, inflammatory glandular diseases or disorders, inflammatory UM-43148.601 gastrointestinal diseases or disorders, inflammatory cutaneous diseases or disorders, inflammatory hepatic diseases or disorders, inflammatory neurological diseases or disorders, inflammatory musculo-skeletal diseases or disorders, inflammatory renal diseases or disorders, inflammatory reproductive diseases or disorders, inflammatory systemic diseases or disorders, inflammatory connective tissue diseases or disorders, inflammatory tumors, necrosis, inflammatory implant-related diseases or disorders, inflammatory aging processes, immunodeficiency diseases or disorders, proliferative diseases and disorders, and inflammatory pulmonary diseases or disorders. In certain embodiments, the present invention provides a method for treating and / or preventing diabetes in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. In certain embodiments, the present invention provides a method for treating and / or preventing celiac disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of any of the compositions recited herein. Additional embodiments will be apparent to persons skilled in the relevant art based on the teachings contained herein. BRIEF DESCRIPTION OF THE DRAWINGS FIG.1A-E. Formulation, characterization, and stability of Celastrol-DMPC sHDL Nanoparticles. (A) Gross appearance of celastrol-DMPC sHDL nanoparticle formulation after solubilization of celastrol / 22A / DMPC in glacial acetic acid, lyophilization and overnight rehydration in 10 mM phosphate buffer (pH 7.4) with three 5 minute cycles of heating and cooling at 4 ^C and 40 ^C. (B) Dynamic light scattering measurements of celastrol-DMPC sHDL nanoparticle by intensity after filtration and centrifugal buffer exchange. (C) UV-visible light spectrum of celastrol-DMPC sHDL nanoparticle formulation in a quartz cuvette. (D) Biphenyl RP-HPLC method for analysis of nanoparticle composition and quantification of celastrol loading for determination of drug loading incorporation efficiency. (E) Long-term stability of celastrol-DMPC sHDL nanoparticles stored at 4 ^C via serial DLS measurements to assess nanoparticle diameter by intensity (black marker connected by dashed line; right axis) and polydispersity index (black bars; right axis). FIG.2A-B. Formulation and characterization of Celastrol-DPPC sHDL Nanoparticles. (A) Gross appearance of celastrol-DPPC sHDL nanoparticle formulation after solubilization of celastrol / 22A / DPPC in glacial acetic acid, lyophilization and overnight rehydration in 10 mM phosphate buffer (pH 7.4) with three 5 minute cycles of heating and cooling at 4 ^C and 50 ^C. UM-43148.601 (B) Dynamic light scattering measurements of celastrol-DPPC sHDL nanoparticle diameter distribution by intensity after 0.22 micron filtration and centrifugal buffer exchange. FIG. 3A-C. Quantification of Celastrol loading in DMPC sHDL Nanoparticles via UV- VIS spectroscopy. (A) Ultraviolet-visible spectrum of celastrol standards solubilized in DMSO. (B) Standard curve of DMSO solubilized celastrol quantitation at 424 nm. (C) Quantification of celastrol loading in sHDL nanoparticles via measurement at 424 nm. FIG. 4A-D. RAW 264.7 cells stimulated with LPS (1 µg / mL) in setting of varying concentrations of celastrol to assess effects on (A) nitrite (B) IL-6 cytokine measurements (C) TNF-α cytokine measurements and (D) MTS cell viability assessment. FIG. 5A-D. Inhibition of NF-κB Activation by Celastrol in THP-1 NF-κB Reporter Cell Line and Cytotoxicity. (A) Celastrol-DMPC sHDL nanoparticle dose response curve in LPS (50 ng / mL) stimulated THP-1 NF-κB reporter line. (B) Controls of PBS, DMSO (0.01%) and blank DMPC sHDL nanoparticles in LPS (50 ng / mL) THP-1 cells. (C) IC50 calculation of celastrol dose response curve. (D) THP-1 MTS cytotoxicity assessment at different concentrations of free celastrol (DMSO), celastrol DMPC sHDL nanoparticles, and controls. FIG.6A-B. Effects of Celastrol-DMPC sHDL Nanoparticles on Inflammatory Responses in Human Fibroblast-Like Synoviocytes (FLS) (A) Celastrol-DMPC sHDL nanoparticles dose response inhibition of IL-6, TNF-α and MCP-1 cytokine in FLS cells stimulated with IL-1β (10 ng / mL). (B) Celastrol-DMPC sHDL nanoparticles dose response inhibition of IL-6, TNF-α and MCP-1 cytokine in FLS cells stimulated with TNF-α (10 ng / mL). FIG.7A-B. (A) This shows schematic representation of the experimental design for the ZIA model. Mice were pre-treated with PBS or celastrol-loaded DMPC sHDL nanoparticles (1 mg / kg celastrol) prior to intra-articular injection of zymosan. (B) Joint swelling was assessed by measuring the change in medial-to-lateral joint diameter. Mice pre-treated with Cel-DMPC sHDL nanoparticles exhibited significantly reduced joint swelling compared to PBS-treated controls. Data are presented as mean ± SEM; ** denotes p < 0.01 by unpaired t-test. FIG.8A-B. (A) This shows schematic representation of the CIA experimental setup. Mice were immunized with type II collagen emulsified in complete Freund's adjuvant (CFA) on Day 0 and boosted with type II collagen in incomplete Freund's adjuvant (IFA) on Day 21. Upon clinical arthritis onset (Day 25–31), mice were treated with celastrol-loaded nanodiscs (1 mg / kg celastrol) every other day. (B) Arthritis severity was assessed every other day using a composite clinical arthritis score. Therapeutic administration of Celasterol-sHDL nanoparticles significantly reduced disease severity. Data are shown as mean ± SEM, **** denotes p < 0.0001 by two-way ANOVA with Tukey’s post-hoc test. UM-43148.601 FIG.9A-B. (A) illustrates the loading sequence of sHDL nanoparticles with antigen peptides and rapamycin. (B) shows that rapamycin-antigen-DMPC sHDL nanoparticle size via DLS demonstrated a narrowly distributed size range (7-10 nm) after 0.22 micron filtration and centrifugal ultrafiltration, suggesting uniform particle sizes conducive to consistent drug delivery. FIG.10. This shows stacked chromatograms illustrating confirmation of antigen and rapamycin drug loading after methanol disruption of nanoparticle assembly via an analytical biphenyl RP-HPLC for separation of nanoparticle components. The bottommost chromatogram demonstrates successful separation of 22A (scaffolding peptide), rapamycin, antigen-lipid conjugate, and DMPC (phospholipid) at 220 nm absorbance. Upper chromatograms are representative chromatograms of standards for each component. FIG.11A-B. (A) BMDCs were treated with nanoparticles loaded with rapamycin and OVA323-339 (OVA-II) peptide for 24 hours and cocultured with CD4+ T cells from OT-II transgenic mice under Treg-inducing conditions for 5 days. (B) BMDCs were treated with OVA-II peptide with or without rapamycin at increasing concentrations of 5, 50, 500 ng / mL and 1, 10, 100 ng / mL, respectively. FIG.12A-B. (A) OT-II+Thy1.1+CD4+ T cells were adoptively transferred to naïve C57BL / 6 mice, followed by administration of nanoparticles loaded with 13 ug rapamycin and 100 ug OVA-II peptide 1 day after the transfer. (B) Analysis of peripheral blood mononuclear cells (PBMCs) 5 days after the nanoparticle administration shows the frequencies of donor OT- II+Thy1.1+CD4+ T cells and donor OT-IIThy1.1+CD4+Foxp3+ Tregs in PBMCs. DEFINITIONS The term “about” is used herein to mean a value that is ±10% of the recited value. As used herein, by “administering” is meant a method of giving a dosage of a composition described herein to a subject. The compositions utilized in the methods described herein can be administered by any suitable route, including, for example, by inhalation, nebulization, aerosolization, intranasally, intratracheally, intrabronchially, orally, parenterally (e.g., intravenously, subcutaneously, or intramuscularly), orally, nasally, rectally, topically, or buccally. The compositions utilized in the methods described herein can also be administered locally or systemically. The preferred method of administration can vary depending on various factors (e.g., the components of the composition being administered, and the severity of the condition being treated). UM-43148.601 As used herein, the term “associated with” refers to the state of two or more entities (e.g., nanoparticles and one or more peptides) which are linked by a direct or indirect covalent or non- covalent interaction. In some embodiments, an association is covalent. In some embodiments, a covalent association is mediated by a linker moiety. In some embodiments, an association is non-covalent (e.g., charge interactions, affinity interactions, metal coordination, physical adsorption, host-guest interactions, hydrophobic interactions, TT stacking interactions, hydrogen bonding interactions, van der Waals interactions, magnetic interactions, electrostatic interactions, dipole-dipole interactions, etc.). For example, in some embodiments, a peptide is admixed with a nanoparticle. In some embodiments, a peptide is conjugated with a nanoparticle. In some embodiments, a peptide is encapsulated within a nanoparticle. In some embodiments, a peptide is absorbed into a nanoparticle. In some embodiments, a peptide is adsorbed onto a nanoparticle. In some embodiments, a peptide is admixed with a nanoparticle. As used herein, the term “absorbed” refers to a peptide that is taken into and stably retained in the interior, that is, internal to the outer surface, of a nanoparticle and / or microparticle. As used herein, the term “admixed” refers to a peptide that is dissolved, dispersed, or suspended in a nanoparticle and / or microparticle. In some cases, the biomacromolecule agent may be uniformly admixed in the nanoparticle and / or microparticle. As used herein, the term “adsorbed” refers to the attachment of a peptide to the external surface of a nanoparticle and / or microparticle. Such adsorption preferably occurs by electrostatic attraction. Electrostatic attraction is the attraction or bonding generated between two or more oppositely charged or ionic chemical groups. Generally, the adsorption is typically reversible. As used herein, the term “HDL” or “high density lipoprotein” refers to high-density lipoprotein. HDL comprises a complex of lipids and proteins in approximately equal amounts that functions as a transporter of cholesterol in the blood. HDL is mainly synthesized in and secreted from the liver and epithelial cells of the small intestine. Immediately after secretion, HDL is in a form of a discoidal particle containing apolipoprotein A-I (also called apoA-I) and phospholipid as its major constituents and is also called nascent HDL. This nascent HDL receives, in blood, free cholesterol from cell membranes of peripheral cells or produced in the hydrolysis course of other lipoproteins, and forms mature spherical HDL while holding, at its hydrophobic center, cholesterol ester converted from said cholesterol by the action of LCAT (lecithin cholesterol acyltransferase). HDL plays an extremely important role in a lipid metabolism process called “reverse cholesterol transport”, which takes, in blood, cholesterol out UM-43148.601 of peripheral tissues and transports it to the liver. High levels of HDL are associated with a decreased risk of atherosclerosis and coronary heart disease (CHD) as the reverse cholesterol transport is considered one of the major mechanisms for HDL’s prophylactic action on atherosclerosis. As used herein, the term “nucleic acid” may be DNA or RNA, such as mRNA. In embodiments, the compositions comprise a complement, such as a full-length complement, or a degenerate (due to degeneracy of the genetic code) of any of the nucleic acids provided herein. In embodiments, the nucleic acid is an expression vector that can be transcribed when transfected into a cell line. In embodiments, the expression vector may comprise a plasmid, retrovirus, or an adenovirus amongst others. Nucleic acids can be isolated or synthesized using standard molecular biology approaches, for example by using a polymerase chain reaction to produce a nucleic acid fragment, which is then purified and cloned into an expression vector. Additional techniques useful in the practice of this invention may be found in Current Protocols in Molecular Biology 2007 by John Wiley and Sons, Inc.; Molecular Cloning: A Laboratory Manual (Third Edition) Joseph Sambrook, Peter MacCallum Cancer Institute, Melbourne, Australia; David Russell, University of Texas Southwestern Medical Center, Dallas, Cold Spring Harbor. As used herein, the term “in vitro” refers to an artificial environment and to processes or reactions that occur within an artificial environment. In vitro environments can consist of, but are not limited to, test tubes and cell culture. The term “in vivo” refers to the natural environment (e.g., an animal or a cell) and to processes or reaction that occur within a natural environment. As used here, the term “lipids” or “lipid molecules” refer to fatty substances that are insoluble in water and include fats, oils, waxes, and related compounds. They may be either made in the blood (endogenous) or ingested in the diet (exogenous). Lipids are essential for normal body function and whether produced from an exogenous or endogenous source, they must be transported and then released for use by the cells. The production, transportation, and release of lipids for use by the cells is referred to as lipid metabolism. While there are several classes of lipids, two major classes are cholesterol and triglycerides. Cholesterol may be ingested in the diet and manufactured by the cells of most organs and tissues in the body, primarily in the liver. Cholesterol can be found in its free form or, more often, combined with fatty acids forming what is known as cholesterol esters. As used herein, “lipid” or “lipid molecule” refers to any lipophilic compound. Non-limiting examples of lipid compounds include fatty acids, cholesterol, phospholipids, complex lipids, and derivatives or analogs UM-43148.601 thereof. They are usually divided into at least three classes: (1) “simple lipids,” which include fats and oils as well as waxes; (2) “compound lipids,” which include phospholipids and glycolipids; and (3) “derived lipids” such as steroids. Lipids or lipid molecules suitable for use in the present invention include both membrane-forming lipids and non-membrane-forming lipids. As used herein the term, “lipoproteins” refer to compounds that are structured so that water-insoluble lipids are contained in a partially water-soluble shell. Depending on the type of lipoprotein, the contents include varying amounts of free and esterified cholesterol, triglycerides, and apoproteins or apolipoproteins. There are five major types of lipoproteins, which differ in function and in their lipid and apoprotein content and are classified according to increasing density: (i) chylomicrons and chylomicron remnants, (ii) very low density lipoproteins (“VLDL”), (iii) intermediate-density lipoproteins (“IDL”), (iv) low-density lipoproteins (“LDL”), and (v) high-density lipoproteins (“HDL”). Cholesterol circulates in the bloodstream as particles associated with lipoproteins. By “pharmaceutical composition” is meant any composition that contains a peptide that is suitable for administration to a subject. Any formulation can be prepared by well-known and accepted methods in the art. See, for example, Remington: The Science and Practice of Pharmacy (21sted.), ed. A.R. Gennaro, Lippincott Williams & Wilkins, 2005, and Encyclopedia of Pharmaceutical Technology, ed. J. Swarbrick, Informa Healthcare, 2006, each of which is hereby incorporated by reference. By “pharmaceutically acceptable diluent, excipient, carrier, or adjuvant” is meant a diluent, excipient, carrier, or adjuvant which is physiologically acceptable to the subject while retaining the therapeutic properties of the pharmaceutical composition with which it is administered. As used herein, the term “sample” is used in its broadest sense. In one sense, it is meant to include a specimen or culture obtained from any source, as well as biological and environmental samples. Biological samples may be obtained from animals (including humans) and encompass fluids, solids, tissues, and gases. Biological samples include blood products, such as plasma, serum and the like. Environmental samples include environmental material such as surface matter, soil, water, crystals, and industrial samples. Such examples are not however to be construed as limiting the sample types applicable to the present invention. As used herein, the term “subject” refers to any animal (e.g., a mammal), including, but not limited to, humans, non-human primates, rodents, and the like, which is to be the recipient of UM-43148.601 a particular treatment. Typically, the terms “subject” and “patient” are used interchangeably herein in reference to a human subject. As used herein, the terms “synthetic HDL,” “sHDL,” “reconstituted HDL”, and “rHDL” refer to a particle structurally analogous to native HDL, composed of a lipid or lipids in association with at least one of the proteins of HDL, preferably ApoA-I, or a mimetic thereof. Typically, the components of sHDL may be derived from blood or produced by recombinant technology. By “therapeutically effective amount” is meant the amount of a composition administered to improve, inhibit, or ameliorate a condition of a subject, or a symptom of a disorder or disease, e.g., celiac disease, in a clinically relevant manner. Any improvement in the subject is considered sufficient to achieve treatment. Preferably, an amount sufficient to treat is an amount that reduces, inhibits, or prevents the occurrence or one or more symptoms of the disease or disorder or is an amount that reduces the severity of, or the length of time during which a subject suffers from one or more symptoms of the disease or disorder (e.g., by at least about 10%, about 20%, or about 30%, more preferably by at least about 50%, about 60%, or about 70%, and most preferably by at least about 80%, about 90%, about 95%, about 99%, or more, relative to a control subject that is not treated with a composition described herein). An effective amount of the pharmaceutical composition used to practice the methods described herein varies depending upon the manner of administration and the age, body weight, and general health of the subject being treated. A physician or researcher can decide the appropriate amount and dosage regimen. As used herein, the term “solvent” refers to a medium in which a reaction is conducted. Solvents may be liquid but are not limited to liquid form. Solvent categories include but are not limited to nonpolar, polar, protic, and aprotic. DETAILED DESCRIPTION OF THE INVENTION Experiments conducted during the course of developing embodiments for the present invention resulted in the formulation and characterization of Celastrol-DMPC sHDL nanoparticles and Celastrol-DPPC sHDL nanoparticles. Such experiments further quantified Celastrol loading in DMPC sHDL nanoparticles via UV-VIS spectroscopy. In addition, such experiments demonstrate the effects of Celastrol on RAW 264.7 macrophage cell line stimulation response, and inhibition of NF-κB activation by Celastrol in THP-1 NF-κB reporter cell line and cytotoxicity assessment. The effects of Celastrol-DMPC sHDL nanoparticles on UM-43148.601 inflammatory responses in human fibroblast-like synoviocytes (FLS) were additionally demonstrated in such experiments. Accordingly, the present invention relates to compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol and / or rapamycin. In particular, the present invention relates to nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, and related methods of use (e.g., in diagnostic and / or therapeutic settings). Accordingly, in certain embodiments, the present invention provides compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol (or variants thereof). The traditional Chinese medicine Tripterygium wilfordii is the root of Tripterygium wilfordii Hook.f. in the family Celastraceae, also called Huang-teng, Huang-la-teng, Cai-chong-yao, Hong-yao and Shui-mang- cao, mainly produced in Fujian, Anhui, Zhejiang, Henan and other places in China, and often used for treating diseases such as arthritis, leprosy, eczema, tuberculosis. Celastrol ( hydroxy- tetradecahydropicene-2-carboxylic acid) (also called Tripterine) is an important triterpenoid active ingredient in the traditional Chinese medicine Tripterygium wilfordii, and is widely present in celastraceae plants such as Tripterygium wilfordii Hook.f., Celastrus orbiculatus Thunb., and Celastrus monospermus Roxb. Celastrol has demonstrated good biological activity in researches of anti-inflammation, immunosuppression, anti-tumor, anti- neurodegeneration and weight loss, and has broad development prospects. In certain embodiments, the present invention provides compositions comprising nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) rapamycin (or variants thereof). Rapamycin ( UM-43148.601 ), also known as sirolimus, is a macrocyclic lactone antibiotic immunosuppressive agent. Clinically, it is used for anti-rejection in organ transplantation and treatment of autoimmune diseases. It exhibits immunosuppressive activity tens of times stronger than the widely used cyclosporine, with low toxicity and a small dosage (2 mg / day / person), it exhibits synergistic immunosuppressive effects when used in combination with cyclosporine clinically. Compared to cyclosporine and FK506 (tacrolimus), sirolimus has the lowest renal toxicity among other immunosuppressive agents and no neurotoxicity. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle associated with celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises a mixture of at least one phospholipid and at least one HDL apolipoprotein or apolipoprotein mimetic, wherein the sHDL nanoparticle is optionally further associated with a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), at least one phospholipid selected from 1,2-dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC), at least one HDL apolipoprotein or apolipoprotein mimetic, and optionally a plurality of tolerogenic antigens. In certain embodiments, the present invention provides a composition comprising an sHDL nanoparticle comprising celastrol (or variant thereof) and / or rapamycin (or a variant thereof), at least one phospholipid selected from 1,2-dimyristol-sn-glycero-3-phosphocholine UM-43148.601 (DPMC) and dipalmitoylphosphatidylcholine (DPPC) and at least one HDL apolipoprotein or apolipoprotein mimetic, and a plurality of tolerogenic antigens. The present invention is not limited to specific types or kinds of nanoparticles associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) celastrol (or variants thereof) and / or rapamycin (or variants thereof). Examples of nanoparticles include, but are not limited to, fullerenes (a.k.a. C60, C70, C76, C80, C84), endohedral metallofullerenes (EMI's) buckyballs, which contain additional atoms, ions, or clusters inside their fullerene cage), trimetallic nitride templated endohedral metallofullerenes (TNT EMEs, high-symmetry four-atom molecular cluster endohedrals, which are formed in a trimetallic nitride template within the carbon cage), single-walled and mutli- walled carbon nanotubes, branched and dendritic carbon nanotubes, gold nanorods, silver nanorods, single-walled and multi-walled boron / nitrate nanotubes, carbon nanotube peapods (nanotubes with internal metallo-fullerenes and / or other internal chemical structures), carbon nanohorns, carbon nanohorn peapods, liposomes, nanoshells, dendrimers, quantum dots, superparamagnetic nanoparticles, nanorods, and cellulose nanoparticles. The particle embodiment can also include microparticles with the capability to enhance effectiveness or selectivity. Other non-limiting exemplary nanoparticles include glass and polymer micro- and nano-spheres, biodegradable PLGA micro- and nano-spheres, gold, silver, carbon, and iron nanoparticles. In some embodiments, the nanoparticle is a modified micelle. In these embodiments, the modified micelle comprises polyol polymers modified to contain a hydrophobic polymer block. The term “hydrophobic polymer block” as used in the present disclosure indicates a segment of the polymer that on its own would be hydrophobic. The term “micelle” as used herein refers to an aggregate of molecules dispersed in a liquid. A typical micelle in aqueous solution forms an aggregate with the hydrophilic “head” regions in contact with surrounding solvent, sequestering the hydrophobic single tail regions in the micelle centre. In some embodiments the head region may be, for example, a surface region of the polyol polymer while the tail region may be, for example, the hydrophobic polymer block region of the polyol polymer. The invention further encompasses use of particles on the micrometer scale in addition to the nanometer scale. Where microparticles are used, it is preferred that they are relatively small, on the order of 1-50 micrometers. For ease of discussion, the use herein of “nanoparticles” encompasses true nanoparticles (sizes of from about 1 nm to about 1000 nm), microparticles (e.g., from about 1 micrometer to about 50 micrometers), or both. UM-43148.601 Examples of nanoparticles include, by way of example and without limitation, paramagnetic nanoparticles, superparamagnetic nanoparticles, metal nanoparticles, fullerene-like materials, inorganic nanotubes, dendrimers, dendrimers with covalently attached metal chelates, nanofibers, nanohorns, nano-onions, nanorods, nanoropes and quantum dots. In some embodiments, a nanoparticle is a metal nanoparticle (for example, a nanoparticle of gold, palladium, platinum, silver, copper, nickel, cobalt, iridium, or an alloy of two or more thereof). Nanoparticles can include a core or a core and a shell, as in core- shell nanoparticles. In some embodiments, the nanoparticles are sHDL nanoparticles. Generally, sHDL nanoparticles are composed of a mixture of HDL apolipoprotein and an amphipathic lipid. The present invention is not limited to use of a particular type or kind of HDL apolipoprotein. HDL apolipoproteins include, for example apolipoprotein A-I (apo A-I), apolipoprotein A-II (apo A-II), apolipoprotein A4 (apo A4), apolipoprotein Cs (apo Cs), and apolipoprotein E (apo E). In some embodiments, the HDL apolipoprotein is selected from preproapoliprotein, preproApoA-I, proApoA-I, AρoA-I, preproApoA-II, proApoA-II, ApoA-II, preproApoA-lV, proApoA-lV, ApoA-IV, ApoA-V, preproApoE, proApoE, ApoE, preproApoA- lMilano, ρroApoA-IMilano ApoA-lMilano ρreproApoA-IParis , proApoA-IParis, and ApoA- IParis and peptide mimetics of these proteins mixtures thereof. Preferably, the carrier particles are composed of Apo A-I or Apo A-II, however the use of other lipoproteins including apolipoprotein A4, apolipoprotein Cs or apolipoprotein E may be used alone or in combination to formulate carrier particle mixtures for delivery of therapeutic agents. In some embodiments, mimetics of such HDL apolipoproteins are used. ApoA-I is synthesized by the liver and small intestine as preproapolipoprotein which is secreted as a proprotein that is rapidly cleaved to generate a mature polypeptide having 243 amino acid residues. ApoA-I consists mainly of 6 to 8 different 22 amino acid repeats spaced by a linker moiety which is often proline, and in some cases consists of a stretch made up of several residues. ApoA-I forms three types of stable complexes with lipids: small, lipid-poor complexes referred to as pre-beta-1 HDL; flattened discoidal particles containing polar lipids (phospholipid and cholesterol) referred to as pre-beta-2 HDL; and spherical particles containing both polar and nonpolar lipids, referred to as spherical or mature HDL (HDL3and HDL2). Most HDL in the circulating population contain both ApoA-I and ApoA-II (the second major HDL protein). In some embodiments, ApoA-I agonists or mimetics are provided. In some embodiments, such ApoA-I mimetics are capable of forming amphipathic α-helices that mimic the activity of ApoA-I, and have specific activities approaching or exceeding that of the native molecule. In some, the ApoA-I mimetics are peptides or peptide analogues that: form UM-43148.601 amphipathic helices (in the presence of lipids), bind lipids, form pre-β-like or HDL-like complexes, activate lecithin:cholesterol acyltransferase (LCAT), increase serum levels of HDL fractions, and promote cholesterol efflux. The present invention is not limited to use of a particular ApoA-I mimetic. In some embodiments, any of the ApoA-I mimetics described in Srinivasa, et al., 2014 Curr. Opinion Lipidology Vol.25(4): 304-308 are utilized. In some embodiments, any of the ApoA-I mimetics described in U.S. Patent Application Publication Nos.20110046056 and 20130231459 are utilized. In some embodiments, the “22A” ApoA-I mimetic is used (PVLDLFRELLNELLEALKQKLK) (SEQ ID NO: 4) (see, e.g., U.S. Patent No.7,566,695). In some embodiments, any of the following ApoA-I mimetics shown in Table 1 as described in U.S. Patent No.7,566,695 are utilized: Table 1. ApoA-I mimetics SEQ ID NO AMINO ACID SEQUENCE (SEQ ID NO:1) PVLDLFRELLNELLEZLKQKLK UM-43148.601 (SEQ ID NO:25) PVLDFFRELLNEXLEALKQKLK (SEQ ID NO:26) PVLDLFRELLNELLELLKQKLK UM-43148.601 (SEQ ID NO:67) ~VLDLFRELLNELLEALKQKLK (SEQ ID NO:68) PVLDEFRELLKEXLEALKQKLK UM-43148.601 (SEQ ID NO:109) PVLDEFREKLNERLEALKQKLK (SEQ ID NO:110) PVLDEFREKLNEXXEALKQKLK UM-43148.601 (SEQ ID NO:151) PVLELFENLGERLLDALQKKLK (SEQ ID NO:152) PVFELFENLLERLLDALQKKLK UM-43148.601 (SEQ ID NO:193) PVLDLFRELLEELKQKLK* (SEQ ID NO:194) PVLELFRELLEELKQKLK* UM-43148.601 (SEQ ID NO:235) EWLEAFYKKVLEKLKELF* (SEQ ID NO:236) DWLKAFYDKVAEKLKEAF* indicates peptides that are N-terminal dansylated; sp indicates peptides that exhibited solubility problems under the experimental conditions; X is Aib; Z is Nal; O is Orn; He (%) designates percent helicity; mics designates micelles; and ˜ indicates deleted amino acids. In some embodiments, an ApoA-I mimetic having the following sequence as described in U.S. Patent No.6,743,778 is utilized: Asp Trp Leu Lys Ala Phe Tyr Asp Lys Val Ala Glu Lys Leu Lys Glu Ala Phe (SEQ ID NO:255). In some embodiments, any of the following ApoA-I mimetics shown in Table 2 as described in U.S. Patent Application Publication No.2003 / 0171277 are utilized: Table 2. SEQ ID NO AMINO ACID SEQUENCE UM-43148.601 (SEQ ID NO:262) Ac-D-W-L-K-A-F-Y-D-K-F-F-E-K-F-K-E-F-F-NH2 (SEQ ID NO:263) Ac-D-W-F-K-A-F-Y-D-K-F-F-E-K-F-K-E-F-F-NH2 UM-43148.601 (SEQ ID NO:296) Ac-D-W-F-K-A-F-Y-E-K-F-F-E-K-F-K-E-F-F-NH2 (SEQ ID NO:297) Ac-E-W-L-K-A-L-Y-E-K-V-A-E-K-L-K-E-A-L-NH2 UM-43148.601 (SEQ ID NO:330) Ac-E-W-L-K-A-F-Y-E-K-V-A-E-R-L-R-E-A-F-NH2 (SEQ ID NO:331) Ac-D-W-L-R-A-F-Y-D-K-V-A-E-R-L-K-E-A-F-NH2 In some embodiments, an ApoA-I mimetic having the following sequence as described in U.S. Patent Application Publication No.2006 / 0069030 is utilized: F-A-E-K-F-K-E-A-V-K- D-Y-F-A-K-F-W-D (SEQ ID NO:333). In some embodiments, an ApoA-I mimetic having the following sequence as described in U.S. Patent Application Publication No.2009 / 0081293 is utilized: DWFKAFYDKVAEKFKEAF (SEQ ID NO: 334); DWLKAFYDKVAEKLKEAF (SEQ ID NO: 335); PALEDLRQGLLPVLESFKVFLSALEEYTKKLNTQ (SEQ ID NO: 336). In some embodiments, an ApoA-I mimetic having one of the following sequences is utilized: WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341), LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358), LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ UM-43148.601 ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373). In some embodiments, the apolipoprotein mimetic is an ApoA-I mimetic, having a sequence of any of SEQ ID NOs: 1-336 and WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341), LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358), LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373). Amphipathic lipids include, for example, any lipid molecule which has both a hydrophobic and a hydrophilic moiety. Examples include phospholipids or glycolipids. UM-43148.601 Examples of phospholipids which may be used in the sHDL nanoparticles (e.g., associated with celastrol and / or rapamycin) include but are not limited to 1,2-dilauroyl-sn-glycero-3- phosphocholine; 1,2-dimyristoyl-sn-glycero-3-phosphocholine; 1,2-dipalmitoyl-sn-glycero-3- phosphocholine; 1,2-distearoyl-sn-glycero-3-phosphocholine; 1,2-diarachidoyl-sn-glycero-3- phosphocholine; 1,2-dibehenoyl-sn-glycero-3-phosphocholine; 1,2-dilignoceroyl-sn-glycero-3- phosphocholine; 1,2-dimyristoleoyl-sn-glycero-3-phosphocholine; 1,2-dimyristelaidoyl-sn- glycero-3-phosphocholine; 1,2-dipalmitoleoyl-sn-glycero-3-phosphocholine; 1,2- dipalmitelaidoyl-sn-glycero-3-phosphocholine; 1,2-dipetroselenoyl-sn-glycero-3- phosphocholine; 1,2-dioleoyl-sn-glycero-3-phosphocholine; 1,2-dielaidoyl-sn-glycero-3- phosphocholine; 1,2-dieicosenoyl-sn-glycero-3-phosphocholine; 1,2-dinervonoyl-sn-glycero-3- phosphocholine; 1,2-dilauroyl-sn-glycero-3-phosphoethanolamine; 1,2-dimyristoyl-sn-glycero- 3-phosphoethanolamine; 1,2-dipentadecanoyl-sn-glycero-3-phosphoethanolamine; 1,2- dipalmitoyl-sn-glycero-3-phosphoethanolamine; 1,2-distearoyl-sn-glycero-3- phosphoethanolamine; 1,2-dipalmitoleoyl-sn-glycero-3-phosphoethanolamine; 1,2-dielaidoyl- sn-glycero-3-phosphoethanolamine; 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine; dioleoyl- sn-glycero-3-phosphoethanolamine-N-[3-(2-pyridyldithio) propionate]; 1,2-dipalmitoyl-sn- glycero-3-phosphothioethanol; 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine-N- [4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine- N-[4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn-glycero-3- phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]; 1,2-di-(9Z- octadecenoyl)-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane- carboxamide]; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Distearoyl; N-[(3-Maleimide-1- oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N- (3-Maleimide-1-oxopropyl)-L-α-phosphatidylethanolamine, Dimyristoy; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Dioleoyl; N-(3-Maleimide-1-oxopropyl)-L-α- phosphatidylethanolamine, Dipalmitoyl; N-(3-Maleimide-1-oxopropyl)-L-α- phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; phosphatidylcholine; phosphatidylinositol; phosphatidylserine; phosphatidylethanolamine; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Distearoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dioleoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; N-(Succinimidyloxy-glutaryl)-L-α- UM-43148.601 phosphatidylethanolamine, Dipalmitoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dimyristoyl; 3-(N-succinimidyloxyglutaryl)aminopropyl, and polyethyleneglycol-carbamyl distearoylphosphatidyl-ethanolamine; N-(3-oxopropoxy polyethyleneglycol)carbamyl-distearoyl-ethanolamine. In some embodiments, the amphipathic lipids include but are not limited to dipalmitoylphosphatidylcholine (DPPC), dioleoyl-sn-glycero-3-phosphoethanolamine-N-[3-(2- pyridyldithio) propionate] (DOPE-PDP), 1,2-dipalmitoyl-sn-glycero-3-phosphothioethanol, 1,2- di-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine-N-[4-(p- maleimidophenyl)butyramide], 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p- maleimidophenyl)butyramide], 1,2-dihexadecanoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p- maleimidomethyl)cyclohexane-carboxamide], 1,2-di-(9Z-octadecenoyl)-sn-glycero-3- phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide], phosphatidylcholine, phosphatidylinositol, phosphatidylserine, phosphatidylethanolamine, and combinations thereof. In some embodiments, the phospholipid is complexed with an imaging agent (e.g., rhodamine (Rhod)-labeled DOPE (DOPE-Rhod)). In some embodiments, the phospholipids are thiol reactive phospholipids such as, for example, Dioleoyl-sn-glycero-3- phosphoethanolamine-N-[3-(2-pyridyldithio) propionate] (DOPE-PDP), 1,2-dihexadecanoyl-sn- glycero-3-phosphothioethanol, or N-4-(p-maleimidophenyl)butyryl) dipalmitoylphosphatidylethanolamine (MPB-DPPE)). In some embodiments, exemplary phospholipids include, but are not limited to, small alkyl chain phospholipids, egg phosphatidylcholine, soybean phosphatidylcholine, dipalmitoylphosphatidylcholine, dimyristoylphosphatidylcholine, distearoylphosphatidylcholine 1-myristoyl-2-palmitoylphosphatidylcholine, 1-palmitoyl-2-myristoylphosphatidylcholine, 1- palmitoyl-2-stearoylphosphatidylcholine, 1-stearoyl-2-palmitoylphosphatidylcholine, dioleoylphosphatidylcholine dioleophosphatidylethanolamine, dilauroylphosphatidylglycerol phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylglycerols, diphosphatidylglycerols such as dimyristoylphosphatidylglycerol, dipalmitoylphosphatidylglycerol, distearoylphosphatidylglycerol, dioleoylphosphatidylglycerol, dimyristoylphosphatidic acid, dipalmitoylphosphatidic acid, dimyristoylphosphatidylethanolamine, dipalmitoylphosphatidylethanolamine, dimyristoylphosphatidylserine, dipalmitoylphosphatidylserine, brain phosphatidylserine, brain sphingomyelin, egg sphingomyelin, milk sphingomyelin, palmitoyl sphingomyelin, phytosphingomyelin, dipalmitoylsphingomyelin, distearoylsphingomyelin, dipalmitoylphosphatidylglycerol salt, phosphatidic acid, galactocerebroside, gangliosides, UM-43148.601 cerebrosides, dilaurylphosphatidylcholine, (1,3)-D-mannosyl-(1,3)diglyceride, aminophenylglycoside, 3-cholesteryl-6′-(glycosylthio)hexyl ether glycolipids, and cholesterol and its derivatives. Phospholipid fractions including SM and palmitoylsphingomyelin can optionally include small quantities of any type of lipid, including but not limited to lysophospholipids, sphingomyelins other than palmitoylsphingomyelin, galactocerebroside, gangliosides, cerebrosides, glycerides, triglycerides, and cholesterol and its derivatives. Phosphatidylethanolamines having a variety of acyl chain groups of varying chain lengths and degrees of saturation can be conjugated to PEG to form the lipid conjugate. Such phosphatidylethanolamines are commercially available, or can be isolated or synthesized using conventional techniques known to those of skilled in the art. Phosphatidylethanolamines containing saturated or unsaturated fatty acids with carbon chain lengths in the range of C10to C20 are preferred. Phosphatidylethanolamines with mono- or diunsaturated fatty acids and mixtures of saturated and unsaturated fatty acids can also be used. Suitable phosphatidylethanolamines include, but are not limited to, dimyristoyl- phosphatidylethanolamine (DMPE), dipalmitoyl-phosphatidylethanolamine (DPPE), dioleoylphosphatidylethanolamine (DOPE), and distearoyl-phosphatidylethanolamine (DSPE). In some embodiments, the present disclosure provides compositions comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, wherein the association between the nanoparticle and the celastrol and / or rapamycin is a covalent association. In some embodiments, the covalent association is mediated by a linker moiety. In some embodiments, a linker moiety is used to couple the celastrol and / or rapamycin to the nanoparticle (e.g., amphipathic lipid of the sHDL). Any linker moiety suitable for coupling the celastrol and / or rapamycin to a lipid can be used including, e.g., non-ester containing linker moieties and ester-containing linker moieties. In a preferred embodiment, the linker moiety is a non-ester containing linker moiety. As used herein, the term “non-ester containing linker moiety” refers to a linker moiety that does not contain a carboxylic ester bond (—OC(O)—). Suitable non-ester containing linker moieties include, but are not limited to, amido (— C(O)NH—), amino (—NR—), carbonyl (—C(O)—), carbamate (—NHC(O)O—), urea (— NHC(O)NH—), disulphide (—S—S—), ether (—O—), succinyl (—(O)CCH2CH2C(O)—), succinamidyl (—NHC(O)CH2CH2C(O)NH—), ether, disulphide, as well as combinations thereof (such as a linker containing both a carbamate linker moiety and an amido linker moiety). In a preferred embodiment, a carbamate linker is used to couple the celastrol and / or rapamycin to the lipid. UM-43148.601 In other embodiments, an ester containing linker moiety is used to couple the celastrol and / or rapamycin to the lipid. Suitable ester containing linker moieties include, e.g., carbonate (—OC(O)O—), succinoyl, phosphate esters (—O—(O)POH—O—), sulfonate esters, and combinations thereof. In some embodiments, the present disclosure provides compositions comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, wherein the association between the nanoparticle and the celastrol and / or rapamycin is a non-covalent association (e.g., charge interactions, affinity interactions, metal coordination, physical adsorption, host-guest interactions, hydrophobic interactions, TT stacking interactions, hydrogen bonding interactions, van der Waals interactions, magnetic interactions, electrostatic interactions, dipole-dipole interactions, etc.). In some embodiments, the present disclosure provides compositions comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, wherein the association between the nanoparticle and the celastrol and / or rapamycin is such that the celastrol and / or rapamycin is admixed with the nanoparticle. In some embodiments, the present disclosure provides compositions comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, wherein the association between the nanoparticle and the celastrol and / or rapamycin is such that the celastrol and / or rapamycin is encapsulated within the nanoparticle. In some embodiments, the present disclosure provides compositions comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamycin, wherein the association between the nanoparticle and the celastrol and / or rapamycin is such that the celastrol and / or rapamycin is adsorbed onto or into the nanoparticle. In some embodiments, the nanoparticles associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) are further associated with a peptide antigen. Such embodiments are not limited to particular antigen. Indeed, antigens can be peptides, proteins, polysaccharides, saccharides, lipids, glycolipids, nucleic acids, or combinations thereof. The antigen can be derived from any source, including, but not limited to, a virus, bacterium, parasite, plant, protozoan, fungus, tissue or transformed cell such as a cancer or leukemic cell and can be a whole cell or immunogenic component thereof, e.g., cell wall components or molecular components thereof. In some embodiments, the antigen is a plurality of tolerogenic antigens (e.g., between 1 – 30 tolerogenic antigens (e.g., 8 – 30 tolerogenic antigens per nanoparticle). In some embodiments, the tolerogenic antigens are antigens that have been identified to UM-43148.601 play a role in autoimmune disease (e.g., MS or celiac disease). In some embodiments, the tolerogenic antigen is between about 3 amino acids and about 50 amino acids in length (e.g., 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, or 50 amino acids in length). In some embodiments, the tolerogenic antigen is a single tolerogenic antigen between about 3 and about 50 amino acids in length. In celiac disease, the main antigens are tissue transglutaminase and gliadin (e.g., α-, γ-, and ω-gliadin). Any antigen identified as a tissue transglutaminase or a gliadin antigen may be used. In some embodiments, the antigen associated with the nanoparticle includes a gliadin polypeptide, such as the full-length gliadin polypeptide or any epitopes of the gliadin polypeptide. In some embodiments, the antigen associated with the nanoparticle includes a 33- mer polypeptide from α2-gliadin. In some embodiments, the 33-mer gliadin polypeptide has at least 90% (at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%) sequence identity to the polypeptide sequence of LQLQPFPQPELPYPQPELPYPQPELPYPQPQPF (SEQ ID NO: 374). In some embodiments, the antigen associated with the nanoparticles includes an epitope of the 33-mer gliadin polypeptide. The epitope of the 33-mer gliadin polypeptide may be a polypeptide of any length shorter than the 33-mer polypeptide, for example the epitope may include between 25 and 3 (e.g., 24, 23, 22, 21, 20, 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, 5, 4 or 3) amino acid residues, between 20 and 5 (e.g., 19, 18, 17, 16, 15, 14, 13, 12, 11, 10, 9, 8, 7, 6, or 5) amino acids residues, between 12 and 6 (e.g., 12, 11, 10, 9, 8, 7 or 6) amino acid residues, or 9 amino acids in length. Further examples of epitopes of the 33-gliadin that may be associated with the nanoparticles include any one of the epitopes described in Table 3, including SEQ ID NOs: 375- 405. In some embodiments, the tolerogenic antigen associated with the nanoparticle may include any one of the antigens described in Table 4, including SEQ ID NOs: 406-580. In some embodiments, the antigen associated with the nanoparticles includes a polypeptide sequence having at least 85% (e.g., at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 95%, or 100%) sequence identity to any one of SEQ ID NOs: 375-580. In some embodiments, the tolerogenic antigen associated with the nanoparticle may include an antigen including two or more (e.g., 2, 3, 4, 5, or 6) polypeptides having the polypeptide sequences of any two of SEQ ID NOs: 375-580. In some embodiments, the plurality of tolerogenic antigens (e.g., between 1 – 30 (e.g., 6 – 30, or 8 – 30 (e.g., 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30)) tolerogenic antigens per nanoparticle) associated with UM-43148.601 the nanoparticles have the same identity as every other tolerogenic antigen associated with the nanoparticle. In some embodiments, the plurality of tolerogenic antigens associated with the nanoparticles includes a population of between 2-10 (e.g., 2, 3, 4, 5, 6, 7, 8, 9, or 10) different antigen sequences implicated in the same disease; for example, the nanoparticles may be associated with between 3-8 (e.g., 3, 4, 5, 6, 7, or 8), 4-6 (e.g., 4, 5, or 6), or 3-4 different polypeptide antigen sequences. In some embodiments, the nanoparticles may be associated with (i) a first polypeptide population comprising the amino acid sequence of any one of SEQ ID NOs: 406-580, or a biologically active fragment or variant thereof, (ii) a second polypeptide population comprising the amino acid sequence of any one of SEQ ID NOs: 406-580, or biologically active fragment or variant thereof, and (iii) a third polypeptide population comprising the amino acid sequence of any one of SEQ ID NOs: 406-580, or a biologically active fragment or variant thereof. In some instances, the first, second, and third polypeptide populations have different amino acid sequences. In some embodiments, the nanoparticles may be associated with (i) a first polypeptide comprising the amino acid sequence LQPFPQPELPYPQPQ (SEQ ID NO: 474), or a biologically active fragment or variant thereof, (ii) a second polypeptide comprising the amino acid sequence QPFPQPEQPFPWQP (SEQ ID NO: 475), or a biologically active fragment or variant thereof, and (iii) a third polypeptide comprising the amino acid sequence PEQPIPEQPQPYPQQ (SEQ ID NO: 476), or a biologically active fragment or variant thereof. In some embodiments, the nanoparticles may be associated with (i) a first polypeptide comprising the amino acid sequence LQPFPQPELPYPQPQ (SEQ ID NO: 474), or a biologically active fragment or variant thereof, (ii) a second polypeptide comprising the amino acid sequence PQQPFPQPEQPFPWQP (SEQ ID NO: 477), or a biologically active fragment or variant thereof, and (iii) a third polypeptide comprising the amino acid sequence FPEQPIPEQPQPYPQQ (SEQ ID NO: 478), or a biologically active fragment or variant thereof. In some embodiments, the nanoparticles may be associated with (i) a first polypeptide comprising the amino acid sequence ELQPFPQPELPYPQPQ (SEQ ID NO: 506), or a biologically active fragment or variant thereof, (ii) a second polypeptide comprising the amino acid sequence EQPFPQPEQPFPWQP (SEQ ID NO: 507), or a biologically active fragment or variant thereof, and (iii) a third polypeptide comprising the amino acid sequence EPEQPIPEQPQPYPQQ (SEQ ID NO: 508), or a biologically active fragment or variant thereof. In some embodiments, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 506, 507, and 508 include an N-terminus pyroglutamic acid (pyroE). In some embodiments described herein, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 506, 507, and 508 include a C-terminus amide UM-43148.601 group. In some embodiments described herein, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 506, 507, and 508 include a N-terminus pyroE residue and a C- terminus amide group. In some embodiments, the nanoparticles may be associated with (i) a first polypeptide comprising the amino acid sequence QLQPFPQPELPYPQPQ (SEQ ID NO: 509), or a biologically active fragment or variant thereof, (ii) a second polypeptide comprising the amino acid sequence QQPFPQPEQPFPWQP (SEQ ID NO: 510), or a biologically active fragment or variant thereof, and (iii) a third polypeptide comprising the amino acid sequence FPEQPIPEQPQPYPQQ (SEQ ID NO: 511), or a biologically active fragment or variant thereof. In some embodiments, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 509, 510, and 511 include an N-terminus acetyl group. In some embodiments described herein, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 509, 510, and 511 include a C-terminus amide group. In some embodiments described herein, the tolerogenic antigens having polypeptide sequences of SEQ ID NOs: 509, 510, and 511 include a N-terminus acetyl group and a C-terminus amide group. In any of the embodiments described herein, the population of antigens associated with the nanoparticle may be fully or partially deamidated. In some embodiments described herein, the tolerogenic antigens associated with the nanoparticle may include an N-terminus pyroglutamic acid (pyroE). In some embodiments described herein, the tolerogenic antigens associated with the nanoparticle may include an N-terminus acetyl group. In some embodiments described herein, the tolerogenic antigens associated with the nanoparticle may include an N-terminus amide group. In some embodiments described herein, the tolerogenic antigens associated with the nanoparticle may include a C-terminus amide group. Table 3: Celiac Disease Relevant T-cell epitopes recognized by CD4+T cells SEQ ID NO: Sequence UM-43148.601 SEQ ID NO: Sequence 385 PQPEQPFCQ Table 4: Tolerogenic Antigens SEQ ID Sequence SEQ ID NO: Sequence P UM-43148.601 SEQ ID Sequence SEQ ID NO: Sequence NO: Q Q UM-43148.601 SEQ ID Sequence SEQ ID NO: Sequence NO: UM-43148.601 SEQ ID Sequence SEQ ID NO: Sequence NO: In some embodiments, the tolerogenic antigen is a biologically active fragment of SEQ ID NO: 474. In some instances, the biologically active fragment of SEQ ID NO: 474 includes a polypeptide comprising the sequence of SEQ ID NO: 512. In some instances, the biologically active fragment of SEQ ID NO: 474 includes a polypeptide comprising the sequence of SEQ ID NO: 580. In some instances, the tolerogenic antigen is a biologically active fragment of SEQ ID NO: 475. In some instances, the biologically active fragment of SEQ ID NO: 475 includes a polypeptide comprising the sequence of SEQ ID NO: 542. UM-43148.601 In some embodiments, the tolerogenic antigen is a biologically active fragment of SEQ ID NO: 476. In some instances, the biologically active fragment of SEQ ID NO: 476 includes a polypeptide comprising the sequence of SEQ ID NO: 563. In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPY (SEQ ID NO: 375). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PYPQPELPY (SEQ ID NO: 376). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPELPYPQ (SEQ ID NO: 377). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FRPEQPYPQ (SEQ ID NO: 378). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQSFPEQQ (SEQ ID NO: 379). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence IQPEQPAQL (SEQ ID NO: 380). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPEQPYPQ (SEQ ID NO: 381). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence SQPEQEFPQ (SEQ ID NO: 382). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQEFPQ (SEQ ID NO: 383). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPEQPFPQ (SEQ ID NO: 384). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFCQ (SEQ ID NO: 385). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPFPEQPQ (SEQ ID NO: 386). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPF (SEQ ID NO: 387). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFPW (SEQ ID NO: 388). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFSEQEQPV (SEQ ID NO: 389). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FSQQQESPF (SEQ ID NO: 390). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPIPEQPQ (SEQ ID NO: 391). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFPQ (SEQ ID NO: 392). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PIPEQPQPY (SEQ ID NO: 393). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQ (SEQ ID NO: 394). In some embodiments, the tolerogenic antigen UM-43148.601 comprises a polypeptide comprising the amino acid sequence PQPEQPFPQ (SEQ ID NO: 395). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PYPEQEEPF (SEQ ID NO: 396). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PYPEQEQPF (SEQ ID NO: 397). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFSEQEQPV (SEQ ID NO: 398). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EGSFQPSQE (SEQ ID NO: 399). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPQQPFPQ (SEQ ID NO: 400). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPQQPYPE (SEQ ID NO: 401). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QGYYPTSPQ (SEQ ID NO: 402). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EGSFQPSQE (SEQ ID NO: 403). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQSFPEQE (SEQ ID NO: 404). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QGYYPTSPQ (SEQ ID NO: 405). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFPW (SEQ ID NO: 406). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPIPV (SEQ ID NO: 407). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFPW (SEQ ID NO: 408). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPIPV (SEQ ID NO: 409). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPFPQ (SEQ ID NO: 410). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LPYPQPQLPYPQ (SEQ ID NO: 411). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LPYPQPELPYPQ (SEQ ID NO: 412). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQLPYPQ (SEQ ID NO: 413). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYPQ (SEQ ID NO: 414). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFSQ (SEQ ID NO: 415). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFSQ (SEQ ID NO: UM-43148.601 416). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFCQ (SEQ ID NO: 417). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFCQ (SEQ ID NO: 418). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQLPYSQ (SEQ ID NO: 419). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYSQ (SEQ ID NO: 420). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQQQCSPVAMPQRLAR (SEQ ID NO: 421). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQLPYLQ (SEQ ID NO: 422). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYLQ (SEQ ID NO: 423). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQFIQPQQPFPQ (SEQ ID NO: 424). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQFIQPEQPFPQ (SEQ ID NO: 425). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LERPWQQQPLPP (SEQ ID NO: 426). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LERPWQEQPLPP (SEQ ID NO: 427). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PIPQQPEQPFPL (SEQ ID NO: 428). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QGQQGYYPISPQQSGQ (SEQ ID NO: 429). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QGQPGYYPTSPQQIGQ (SEQ ID NO: 430). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PGQGQSGYYPTSPQQS (SEQ ID NO: 431). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQTFPQQPQLP (SEQ ID NO: 432). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQTFPEQPQLP (SEQ ID NO: 433). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence GQGQSGYYPTSPQQSG (SEQ ID NO: 434). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QYEVIRSLVLRTLPNM (SEQ ID NO: 435). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QVDPSGQVQWPQ (SEQ ID NO: 436). In some embodiments, the tolerogenic UM-43148.601 antigen comprises a polypeptide comprising the amino acid sequence QVDPSGEVQWPQ (SEQ ID NO: 437). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFPL (SEQ ID NO: 438). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFPL (SEQ ID NO: 439). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPIPY (SEQ ID NO: 440). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPIPY (SEQ ID NO: 441). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPVPQQPQPY (SEQ ID NO: 442). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPVPEQPQPY (SEQ ID NO: 443). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPFPQQPIPQQPQPY (SEQ ID NO: 444). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPIPQQPQPY (SEQ ID NO: 445). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPIPEQPQPY (SEQ ID NO: 446). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQFPQPQQPFPQ (SEQ ID NO: 447). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQFPQPEQPFPQ (SEQ ID NO: 448). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPIPQQPQPYPQQP (SEQ ID NO: 449). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPFPQQPFPQQPQPY (SEQ ID NO: 450). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFSW (SEQ ID NO: 451). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFSW (SEQ ID NO: 452). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPQQPQPYPQQP (SEQ ID NO: 453). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPIPQ (SEQ ID NO: 454). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPIPQ (SEQ ID NO: 455). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPFPQ (SEQ ID NO: 456). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFPQ (SEQ ID NO: UM-43148.601 457). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQPTPI (SEQ ID NO: 458). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPTPI (SEQ ID NO: 459). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PAPIQPQQPFPQ (SEQ ID NO: 460). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PAPIQPEQPFPQ (SEQ ID NO: 461). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPQQPEQI (SEQ ID NO: 462). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPEQPEQI (SEQ ID NO: 463). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPQQPQQI (SEQ ID NO: 464). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPEQPQQI (SEQ ID NO: 465). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQQPEQIISQ (SEQ ID NO: 466). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQQPEQIISQ (SEQ ID NO: 467). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQQPEQIIPQ (SEQ ID NO: 468). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQQPEQIIPQ (SEQ ID NO: 469). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPQQQLPL (SEQ ID NO: 470). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQQLPL (SEQ ID NO: 471). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LFPLPQQPFPQ (SEQ ID NO: 472). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LFPLPEQPFPQ (SEQ ID NO: 473). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELPYPQPQ (SEQ ID NO: 474). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFPWQP (SEQ ID NO: 475). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQPYPQQ (SEQ ID NO: 476). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPFPQPEQPFPWQP (SEQ ID NO: 477). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPEQPIPEQPQPYPQQ UM-43148.601 (SEQ ID NO: 478). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQPYPQQ (SEQ ID NO: 479). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPFLPQLPYPQ (SEQ ID NO: 480). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QAFPQPQQTFPH (SEQ ID NO: 481). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence TPIQPQQPFPQ (SEQ ID NO: 482). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPLQPQQPFPQ (SEQ ID NO: 483). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFTQPQQPTPI (SEQ ID NO: 484). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQLQQPQQP (SEQ ID NO: 485). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence VAHAIIMHQQQQQQQE (SEQ ID NO: 486). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence SYPVQPQQPFPQ (SEQ ID NO: 487). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQQPQPFPQQPVPQQP (SEQ ID NO: 488). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPWQPQQPFPQ (SEQ ID NO: 489). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPLQPQQPFPQ (SEQ ID NO: 490). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPFQPQQPFPQ (SEQ ID NO: 491). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence NPLQPQQPFPLQPQPP (SEQ ID NO: 492). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PLQPQQPFPLQPQPPQ (SEQ ID NO: 493). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PNPLQPQQPFPLQ (SEQ ID NO: 494). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence TIPQQPQQPFPL (SEQ ID NO: 495). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence SFSQQPQQPFPL (SEQ ID NO: 496). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence SFSEQPQQPFPL (SEQ ID NO: 497). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence YSPYQPQQPFPQ (SEQ ID NO: 498). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid UM-43148.601 sequence QLPLQPQQPFPQ (SEQ ID NO: 499). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPQQPFPLQPQQPVP (SEQ ID NO: 500). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence IIPQQPQQPFPL (SEQ ID NO: 501). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQIIPQQPQQP (SEQ ID NO: 502). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FLLQPQQPFSQ (SEQ ID NO: 503). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence IISQQPQQPFPL (SEQ ID NO: 504). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQRPQQPFPQ (SEQ ID NO: 505). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence ELQPFPQPELPYPQPQ (SEQ ID NO: 506). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPFPQPEQPFPWQP (SEQ ID NO: 507). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EPEQPIPEQPQPYPQQ (SEQ ID NO: 508). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QLQPFPQPELPYPQPQ (SEQ ID NO: 509). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QQPFPQPEQPFPWQP (SEQ ID NO: 510). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPEQPIPEQPQPYPQQ (SEQ ID NO: 511). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PELP (SEQ ID NO: 512). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPELPYP (SEQ ID NO: 513). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPELPY (SEQ ID NO: 514). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELP (SEQ ID NO: 515). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PELPYPQP (SEQ ID NO: 516). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPELPYPQ (SEQ ID NO: 517). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPELPYP (SEQ ID NO: 518). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELPY (SEQ ID NO: 519). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELP (SEQ ID NO: 520). UM-43148.601 In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PELPYPQPQ (SEQ ID NO: 521). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPELPYPQP (SEQ ID NO: 522). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELPYP (SEQ ID NO: 523). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPY (SEQ ID NO: 524). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELP (SEQ ID NO: 525). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPELPYPQPQ (SEQ ID NO: 526). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPELPYPQP (SEQ ID NO: 527). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELPYPQ (SEQ ID NO: 528). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPYP (SEQ ID NO: 529). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPY (SEQ ID NO: 530). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELP (SEQ ID NO: 531). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPELPYPQPQ (SEQ ID NO: 532). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELPYPQP (SEQ ID NO: 533). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPYPQ (SEQ ID NO: 534). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYP (SEQ ID NO: 535). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELPY (SEQ ID NO: 536). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPELPYPQPQ (SEQ ID NO: 537). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPYPQP (SEQ ID NO: 538). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELPYP (SEQ ID NO: 539). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPELPYPQPQ (SEQ ID NO: 540). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELPYPQ (SEQ ID NO: 541). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the UM-43148.601 amino acid sequence QPEQPF (SEQ ID NO: 542). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPEQPFP (SEQ ID NO: 543). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPF (SEQ ID NO: 544). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPEQPFPW (SEQ ID NO: 545). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFP (SEQ ID NO: 546). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPEQPF (SEQ ID NO: 547). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPEQPFPWQ (SEQ ID NO: 548). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPEQPFP (SEQ ID NO: 549). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPEQPFPWQP (SEQ ID NO: 550). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFPWQ (SEQ ID NO: 551). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPEQPFPW (SEQ ID NO: 552). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPFP (SEQ ID NO: 553). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPF (SEQ ID NO: 554). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PQPEQPFPWQP (SEQ ID NO: 555). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPEQPFPWQ (SEQ ID NO: 556). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPFPW (SEQ ID NO: 557). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFP (SEQ ID NO: 558). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence FPQPEQPFPWQP (SEQ ID NO: 559). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPFPWQ (SEQ ID NO: 560). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PFPQPEQPFPWQP (SEQ ID NO: 561). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPEQPFPWQ (SEQ ID NO: 562). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PIPEQPQ (SEQ ID NO: 563). In some embodiments, the tolerogenic UM-43148.601 antigen comprises a polypeptide comprising the amino acid sequence PIPEQPQP (SEQ ID NO: 564). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQ (SEQ ID NO: 565). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQP (SEQ ID NO: 566). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PIPEQPQPYP (SEQ ID NO: 567). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQPY (SEQ ID NO: 568). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQP (SEQ ID NO: 569). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQ (SEQ ID NO: 570). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PIPEQPQPYPQQ (SEQ ID NO: 571). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQPYPQ (SEQ ID NO: 572). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQPYP (SEQ ID NO: 573). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQPY (SEQ ID NO: 574). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQPYPQQ (SEQ ID NO: 575). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQPYPQ (SEQ ID NO: 576). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQPYP (SEQ ID NO: 577). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQPYPQQ (SEQ ID NO: 578). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQPYPQ (SEQ ID NO: 579). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PDLP (SEQ ID NO: 580). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PELPYPQ (SEQ ID NO: 581). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYPQP (SEQ ID NO: 582). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPFPQPELPYPQPQ (SEQ ID NO: 583). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence LQPFPQPELPYPQP (SEQ ID NO: 584). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising UM-43148.601 the amino acid sequence PIPEQPQPYPQ (SEQ ID NO: 585). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence QPIPEQPQPYP (SEQ ID NO: 586). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence EQPIPEQPQPY (SEQ ID NO: 587). In some embodiments, the tolerogenic antigen comprises a polypeptide comprising the amino acid sequence PEQPIPEQPQP (SEQ ID NO: 588). In some embodiments, such tolerogenic antigens include human allograft transplantation antigens. Examples of such human allograft transplantation antigens include, but are not limited to, the subunits of the various MHC class I and MHC class II haplotype proteins, and single- amino-acid polymorphisms on minor blood group antigens including RhCE, Kell, Kidd, Duffy and Ss. In some embodiments, the tolerogenic antigen is a self antigen against which a subject (e.g., a human patient) has developed an autoimmune response or may develop an autoimmune response. Examples include proinsulin (e.g., for subjects suffering from or at risk of suffering from diabetes), collagens (e.g., for subjects suffering from or at risk of suffering from rheumatoid arthritis), and myelin basic protein (e.g., for subjects suffering from or at risk of suffering from multiple sclerosis). There are many proteins that are human autoimmune proteins, a term referring to various autoimmune diseases wherein the protein or proteins causing the disease are known or can be established by routine testing. Embodiments include testing a patient to identify an autoimmune protein and creating an antigen for use in a molecular fusion and creating immunotolerance to the protein. Embodiments include an antigen, or choosing an antigen from, one or more of the following proteins. In type 1 diabetes mellitus, several main antigens have been identified: insulin, proinsulin, preproinsulin, glutamic acid decarboxylase-65 (GAD-65), GAD-67, insulinoma-associated protein 2 (IA-2), and insulinoma- associated protein 2β (IA-2β); other antigens include ICA69, ICA12 (SOX-13), carboxypeptidase H, Imogen 38, GLIMA 38, chromogranin-A, HSP-60, carboxypeptidase E, peripherin, glucose transporter 2, hepatocarcinoma-intestine-pancreas / pancreatic associated protein, S100β, glial fibrillary acidic protein, regenerating gene II, pancreatic duodenal homeobox 1, dystrophia myotonica kinase, islet-specific glucose-6-phosphatase catalytic subunit-related protein, and SST G-protein coupled receptors 1-5. In autoimmune diseases of the thyroid, including Hashimoto's thyroiditis and Graves' disease, main antigens include thyroglobulin (TG), thyroid peroxidase (TPO) and thyrotropin receptor (TSHR); other antigens include sodium iodine symporter (NIS) and megalin. In thyroid-associated ophthalmopathy and dermopathy, in addition to thyroid autoantigens including TSHR, an antigen is insulin-like UM-43148.601 growth factor 1 receptor. In hypoparathyroidism, a main antigen is calcium sensitive receptor. In Addison's disease, main antigens include 21-hydroxylase, 17α-hydroxylase, and P450 side chain cleavage enzyme (P450scc); other antigens include ACTH receptor, P450c21 and P450c17. In premature ovarian failure, main antigens include FSH receptor and α-enolase. In autoimmune hypophysitis, or pituitary autoimmune disease, main antigens include pituitary gland-specific protein factor (PGSF) 1a and 2; another antigen is type 2 iodothyronine deiodinase. In multiple sclerosis, main antigens include myelin basic protein, myelin oligodendrocyte glycoprotein and proteolipid protein. In rheumatoid arthritis, a main antigen is collagen II. In immunogastritis, a main antigen is H+, K+-ATPase. In pernicious angemis, a main antigen is intrinsic factor. In celiac disease, main antigens are tissue transglutaminase and gliadin. In vitiligo, a main antigen is tyrosinase, and tyrosinase related protein 1 and 2. In myasthenia gravis, a main antigen is acetylcholine receptor. In pemphigus vulgaris and variants, main antigens are desmoglein 3, 1 and 4; other antigens include pemphaxin, desmocollins, plakoglobin, perplakin, desmoplakins, and acetylcholine receptor. In bullous pemphigoid, main antigens include BP180 and BP230; other antigens include plectin and laminin 5. In dermatitis herpetiformis Duhring, main antigens include endomysium and tissue transglutaminase. In epidermolysis bullosa acquisita, a main antigen is collagen VII. In systemic sclerosis, main antigens include matrix metalloproteinase 1 and 3, the collagen-specific molecular chaperone heat-shock protein 47, fibrillin-1, and PDGF receptor; other antigens include Scl-70, U1 RNP, Th / To, Ku, Jo1, NAG-2, centromere proteins, topoisomerase I, nucleolar proteins, RNA polymerase I, II and III, PM-Slc, fibrillarin, and B23. In mixed connective tissue disease, a main antigen is U1snRNP. In Sjogren's syndrome, the main antigens are nuclear antigens SS-A and SS-B; other antigens include fodrin, poly(ADP-ribose) polymerase and topoisomerase. In systemic lupus erythematosus, main antigens include nuclear proteins including SS-A, high mobility group box 1 (HMGB1), nucleosomes, histone proteins and double-stranded DNA. In Goodpasture's syndrome, main antigens include glomerular basement membrane proteins including collagen IV. In rheumatic heart disease, a main antigen is cardiac myosin. Other autoantigens revealed in autoimmune polyglandular syndrome type 1 include aromatic L-amino acid decarboxylase, histidine decarboxylase, cysteine sulfinic acid decarboxylase, tryptophan hydroxylase, tyrosine hydroxylase, phenylalanine hydroxylase, hepatic P450 cytochromes P4501A2 and 2A6, SOX-9, SOX-10, calcium-sensing receptor protein, and the type 1 interferons interferon alpha, beta and omega. In some cases, the tolerogenic antigen is a foreign antigen against which a patient has developed an unwanted immune response. Examples are food antigens. Embodiments include UM-43148.601 testing a patient to identify foreign antigen and creating a molecular fusion that comprises the antigen and treating the patient to develop immunotolerance to the antigen or food. Examples of such foods and / or antigens are provided. Examples are from peanut: conarachin (Ara h 1), allergen II (Ara h 2), arachis agglutinin, conglutin (Ara h 6); from apple: 31 kDa major allergen / disease resistance protein homolog (Mal d 2), lipid transfer protein precursor (Mal d 3), major allergen Mal d 1.03D (Mal d 1): from milk: α-lactalbumin (ALA), lactotransferrin; from kiwi: actinidin (Act c 1, Act d 1), phytocystatin, thaumatin-like protein (Act d 2), kiwellin (Act d 5); from mustard: 2S albumin (Sin a 1), 11S globulin (Sin a 2), lipid transfer protein (Sin a 3), profilin (Sin a 4); from celery: profilin (Api g 4), high molecular weight glycoprotein (Api g 5); from shrimp: Pen a 1 allergen (Pen a 1), allergen Pen m 2 (Pen m 2), tropomyosin fast isoform; from wheat and / or other cereals: high molecular weight glutenin, low molecular weight glutenin, alpha- and gamma-gliadin, hordein, secalin, avenin; from strawberry: major strawberry allergy Fra a 1-E (Fra a 1), from banana: profilin (Mus xp 1). In some embodiments, the tolerogenic antigens are antigenic peptides of any one of SEQ ID NOs: 589-742 (Table 5). Table 5. Tolerogenic Antigens cont. SEQ ID Sequence Origin g UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: al UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: l UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: UM-43148.601 SEQ ID Sequence Origin NO: In some instances, the autoimmune disease is Type 1 diabetes and the tolerogenic antigen is derived from Carboxypeptidase H, Chromagranin A, Glutamate decarboxylase, Imogen-38, Insulin, Insulinoma antigen-2 and 2β, Islet-specific glucose-6-phosphatase catalytic subunit related protein (IGRP), pancreatic beta-cell antigens or Proinsulin. In some instances, the autoimmune disease is MS and the tolerogenic antigen is derived from α-enolase, aquaporin-4, β-arrestin, myelin basic protein, myelin oligodendrocytic glycoprotein, proteolipid protein, or S100-β. In some instances, the autoimmune disease is rheumatoid arthritis and the tolerogenic antigen is derived from citrullinated protein, collagen II, heat shock proteins, gpl30-RAPS, or human cartilage glycoprotein 39. In some instances, the autoimmune disease is systemic lupus erythematosus and the tolerogenic antigen is derived from La antigen, nucleosome histones and ribonucleoproteins (snRNP), phospholipid-β-2 glycoprotein I complex, poly(ADP-ribose) polymerase, glycoprotein gp70, or Sm antigens of U-1 small ribonucleoprotein complex. In some instances, the autoimmune disease is scleroderma and the tolerogenic antigen is derived from fibrillarin or small nucleolar protein (snoRNP). UM-43148.601 In some embodiments, the autoimmune disease is Graves’ disease and the tolerogenic antigen is derived from thyroid stimulating factor receptor (TSH-R). In some instances, the autoimmune disease is biliary cirrhosis and the tolerogenic antigen is derived from pyruvate dehydrogenase dihydrolipoamide acetyltransferase (PCD-E2). In some embodiments, the autoimmune disease is alopecia areata and the tolerogenic antigen is derived from hair follicle antigens. In some instances, the autoimmune disease is ulcerative colitis and the tolerogenic antigen is derived from human tropomyosin isoform 5 (hTM5). In some instances, the tolerogenic antigen is derived from an antigen selected from a group consisting of 17-hydroxylase, 21-hydroxylase, ADAMTS13, Annexin A5, apoH, AQP4, aromatic acid carboxylase, Basement Membrane Collagen Type IV, BP-1, BP-2, carbonic anhydrase, carboxypeptidase H, cardiolipin, cardiolipin, chromogranin A, complement component 3, Desmoglein 3, enolase, epidermal transglutaminase, GD1a, gliadin, glutamate receptor, Glutamic acid decarboxylase, glycoproteins IIb-IIIa or Ib-IX, GMCSF, gpIIb-IIIa or 1b-IX, GQ1b, GQ1b, histidine-tRNA, histones, HPA-1a, HPA-5b, HSP60, HSP70, HSP90, Hu, IA-2beta, IAPP, ICA69, IFN-gamma, IGRP, IL-1, insulin, insulinoma antigen-2, interferon omega, Jo1, keratin, Kir4.1, LA, LKM-1, LKM-1, LKM-2, LKM-3, LP, major peripheral myelin protein P0, Mi-2, muscarinic acetylcholine receptor M1, MuSK protein; hypocretin, myelin associated glycoprotein (MAG), myelin basic protein (MBP), myelin oligodendrocyte glycoprotein (MOG), myelin-associated oligodendrocytic basic protein cardiac myosin, myeloperoxidase, neurofilaments, nicotinic acetylcholine receptor, orexin, outer surface protein (OSP), p62, phosphatidylserine, proteolipid protein (PLP), pyruvate dehydrogenase, Q-type calcium channel, Ro, sc170, signal recognition peptide, SMA, soluble liver antigen, sp100, synaptogagmin, thyroglobulin, thyroid peroxidase, tissue transglutaminase, TNF-alpha, topoisomerase, transglutaminase, type XVII collagen, U1-RNP, voltage-gated calcium channels, Yo, ZnT8, β2 glycoprotein I, or β2 glycoprotein I. Tolerogenic antigens may further include, but are not limited to, hInsB10-18 (HLVEALYLV (SEQ ID NO: 743)), hIGRP228-236 (LNIDLLWSV (SEQ ID NO: 744)), hIGRP265-273(VLFGLGFAI (SEQ ID NO: 745)), IGRP206-214(VYLKTNVFL (SEQ ID NO: 746)), NRP-A7 (KYNKANAFL (SEQ ID NO: 747)), NRP-I4 (KYNIANVFL (SEQ ID NO: 748)), NRP-V7 (KYNKANVFL (SEQ ID NO: 749)), YAI / Db (FQDENYLYL (SEQ ID NO: 750)) and / or INS B15-23 (LYLVCGERG (SEQ ID NO: 751)), as well as peptides and proteins disclosed in U.S. Publication 20050202032. In certain aspects, a peptide antigen for use in the treatment of type 1 diabetes is UM-43148.601 GAD65114123, VMNILLQYVV (SEQ ID NO: 752); GAD65536-545, RMMEYGTTMV (SEQ ID NO: 753); GFAP143-151, NLAQTDLATV (SEQ ID NO: 754); GFAP214-222, QLARQQVHV (SEQ ID NO: 755); IA-2172-180, SLSPLQAEL (SEQ ID NO: 756); IA-2482-490, SLAAGVKLL (SEQ ID NO: 757); IA-2805-813, VIVMLTPLV (SEQ ID NO: 758); ppIAPP5-13, KLQVFLIVL (SEQ ID NO: 759); ppIAPP9-17, FLIVLSVAL (SEQ ID NO: 760); IGRP152-160, FLWSVFMLI (SEQ ID NO: 761); IGRP211-219, NLFLFLFAV (SEQ ID NO: 762); IGRP215-223, FLFAVGFYL (SEQ ID NO: 763); IGRP222-230, YLLLRVLNI (SEQ ID NO: 764); IGRP228-236, LNIDLLWSV (SEQ ID NO: 744); IGRP265-273, VLFGLGFAI (SEQ ID NO: 745); IGRP293-301, RLLCALTSL (SEQ ID NO: 765); Pro-insulinL2-10, ALWMRLLPL (SEQ ID NO: 766); Pro-insulinL3-11, LWMRLLPLL (SEQ ID NO: 767); Pro-insulinL6-14, RLLPLLALL (SEQ ID NO: 768); Pro- insulinB5-14, HLCGSHLVEA (SEQ ID NO: 769); Pro-insulinB10-18, HLVEALYLV (SEQ ID NO: 743); ProinsulinB14-22, ALYLVCGER (SEQ ID NO: 770); Pro-insulinB15-24, LYLVCGERGF (SEQ ID NO: 771); Pro-insulinB17-25, LVCGERGFF (SEQ ID NO: 772); Pro-insulinB18-27, VCGERGFFYT (SEQ ID NO: 773); Pro-insulinB20-27, GERGFFYT (SEQ ID NO: 774); Pro- insulinB21-29, ERGFFYTPK (SEQ ID NO: 775); Pro-insulinB25-C1, FYTPKTRRE (SEQ ID NO: 776); ProinsulinB27-C5, TPKTRREAEDL (SEQ ID NO: 777); Pro-insulinC20-28, SLQPLALEG (SEQ ID NO: 778); Pro-insulinC25-33, ALEGSLQKR (SEQ ID NO: 779); Pro-insulinC29-A5, SLQKRGIVEQ (SEQ ID NO: 780); Pro-insulinA1-10, GIVEQCCTSI (SEQ ID NO: 781); Pro- insulinA2-10, IVEQCCTSI (SEQ ID NO: 782); Pro-insulinA12-20, SLYQLENYC (SEQ ID NO: 783), or combinations thereof. In still further aspects, tolerogenic antigens associated with multiple sclerosis (MS) can be used and include: MAG287-295, SLLLELEEV (SEQ ID NO: 784); MAG509-517, LMWAKIGPV (SEQ ID NO: 785); MAG556-564, VLFSSDFRI (SEQ ID NO: 786); MBP110-118, SLSRFSWGA (SEQ ID NO: 787); MOG114-122, KVEDPFYWV (SEQ ID NO: 788); MOG166-175, RTFDPHFLRV (SEQ ID NO: 789); MOG172-180, FLRVPCWKI (SEQ ID NO: 790); MOG179-188, KITLFVIVPV (SEQ ID NO: 791); MOG188-196, VLGPLVALI (SEQ ID NO: 792); MOG181-189, TLFVIVPVL (SEQ ID NO: 793); MOG205-214, RLAGQFLEEL (SEQ ID NO: 794); PLP80-88, FLYGALLLA (SEQ ID NO: 795), or combinations thereof. In some instances, tolerogenic antigens associated with systemic lupus erythematosus can be used including, but not limited to, FIEWNKLRFRQGLEW (SEQ ID NO: 796). In some instances, the tolerogenic antigen comprising a polypeptide having the sequence of SEQ ID NO: 796 includes at least one amino acid moiety that is a D-amino acid. Multimeric Tolerogenic Antigens UM-43148.601 In certain embodiments, a tolerogenic antigen provided herein is a multimeric tolerogenic antigen. In one example, a multimeric tolerogenic antigen includes two or more tolerogenic antigens (e.g., a tolerogenic antigen described herein) connected by way or a linker (e.g., a peptide linker). In some instances, the tolerogenic antigen includes the following N- terminal-to-C-terminal structure: (P4-L4)n4-(P3-L3)n3-P2-(L1-P1)n1 Wherein P1, P2, P3, and P4are each independently selected from any tolerogenic antigen described herein (e.g., any tolerogenic antigen from tables 3-5); L1, L3, and L4 are each independently a linker; and n1, n3, and n4are each independently 0 or 1, wherein at least one of n1, n3, and n4 are 1. In some instances, n1is 1, n3is 0, and n4is 0, and the tolerogenic antigen includes the following N-terminal-to-C-terminal structure: P2-L1-P1. In some instances, the peptide linker includes between 2 and 200 amino acids (e.g., between 5 and 50 (e.g., between 5 and 20, 15 and 30, 25 and 40, or 35 and 50), between 45 and 100 (e.g., between 45 and 60, 55 and 70, 65 and 80, 75 and 90, or 85 and 100), 95 and 150 (e.g., between 95 and 110, 105 and 120, 115 and 130, 125 and 140, or 135 and 150), or 145 and 200 amino acids (e.g., between 145 and 160, 155 and 170, 165 and 180, 175 and 190, or 185 and 200)). In some instances, the peptide linker comprises glycine (Gly) and serine (Ser) amino acids. In some instances, the peptide linker includes the amino acid sequence of any one of (GS)x, (GGS)x, (GGGGS (SEQ ID NO: 797))x, (GGSG)x, (SGGG)x, wherein x is an integer from 1 to 10. In certain embodiments the linker includes the amino acid sequence of (GGGGS (SEQ ID NO: 797))x, wherein x is an integer from 2-5. In some instances, P2 and P1 are different tolerogenic antigens. In some instances, P2 and P1 are identical tolerogenic antigens. In some instances, n1 is 1, n3 is 1, and n4 is 0, and the tolerogenic antigen comprises the following N-terminal-to-C-terminal structure: P3-L3-P2-L1-P1. In some instances, each peptide linker independently includes between 2 and 200 amino acids (e.g., between 5 and 50 (e.g., between 5 and 20, 15 and 30, 25 and 40, or 35 and 50), between 45 and 100 (e.g., between 45 and 60, 55 and 70, 65 and 80, 75 and 90, or 85 and 100), 95 and 150 (e.g., between 95 and 110, 105 and 120, 115 and 130, 125 and 140, or 135 and 150), or 145 and 200 amino acids (e.g., between 145 and 160, 155 and 170, 165 and 180, 175 and 190, or 185 and 200)). In some instances, the peptide linker comprises glycine (Gly) and serine (Ser) amino acids. In some instances, the peptide linker includes the amino acid sequence of any one UM-43148.601 of (GS)x, (GGS)x, (GGGGS (SEQ ID NO: 797))x, (GGSG)x, (SGGG)x, wherein x is an integer from 1 to 10. In certain embodiments the linker includes the amino acid sequence of (GGGGS (SEQ ID NO: 797))x, wherein x is an integer from 2-5. In some instances, P3, P2, and / or P1are different tolerogenic antigens. In some instances, P3, P2, and / or P1 are identical tolerogenic antigens. In some instances, n1 is 1, n3 is 1, and n4 is 1, and the tolerogenic antigen comprises the following N-terminal-to-C-terminal structure: P4-L4-P3-L3-P2-L1-P1. In some instances, each peptide linker independently includes between 2 and 200 amino acids (e.g., between 5 and 50 (e.g., between 5 and 20, 15 and 30, 25 and 40, or 35 and 50), between 45 and 100 (e.g., between 45 and 60, 55 and 70, 65 and 80, 75 and 90, or 85 and 100), 95 and 150 (e.g., between 95 and 110, 105 and 120, 115 and 130, 125 and 140, or 135 and 150), or 145 and 200 amino acids (e.g., between 145 and 160, 155 and 170, 165 and 180, 175 and 190, or 185 and 200)). In some instances, the peptide linker comprises glycine (Gly) and serine (Ser) amino acids. In some instances, the peptide linker includes the amino acid sequence of any one of (GS)x, (GGS)x, (GGGGS (SEQ ID NO: 797))x, (GGSG)x, (SGGG)x, wherein x is an integer from 1 to 10. In certain embodiments the linker includes the amino acid sequence of (GGGGS (SEQ ID NO: 797))x, wherein x is an integer from 2-5. In some instances, P4, P3, P2, and / or P1are different tolerogenic antigens. In some instances, P4, P3, P2, and / or P1 are identical tolerogenic antigens. In some embodiments, the tolerogenic antigen is conjugated with the nanoparticle phospholipid in such a manner that facilitates strong immune tolerance upon administration to a subject (e.g., a human subject suffering from or at risk of suffering from an autoimmune disorder (e.g., MS or celiac disease)). In some embodiments, the tolerogenic antigen is conjugated with the nanoparticle phospholipid via a thiol-reactive and reduction-insensitive linkage between the tolerogenic antigen and the nanoparticle phospholipid. Indeed, a thiol-reactive and reduction-insensitive linkage between the tolerogenic antigen and the nanoparticle phospholipid facilitates strong immune tolerance. In some embodiments, the phospholipid is e.g., N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine. In some embodiments, the tolerogenic antigen is conjugated with the nanoparticle phospholipid via an amine-mediated interaction. For example, in some embodiments, the amine-mediated interaction is through an amine-reactive phospholipid (e.g., N- (Succinimidyloxy-glutaryl)-L-α-phosphatidylethanolamine, Dioleoyl (DOPE-NHS)). In some UM-43148.601 embodiments, the amine-mediated interaction is through an amine-reactive phospholipid with self-immolative linkage (e.g., linkers including o-dithiobenzyl, p-dithiobenzyl, beta-dithiobenzyl carbamate moieties, 2,2-dimethyl-4-mercapto- butyric acid, or Disulfide–carbonate-based traceless linker). In some embodiments, the number of tolerogenic antigens associated with a specific nanoparticle is any amount that facilitates strong immune tolerance upon administration to a subject (e.g., a human subject suffering from or at risk of suffering from an autoimmune disorder (e.g., MS or celiac disease). In some embodiments, the amount of tolerogenic antigens associated with a specific nanoparticle is between 1 and 30 (e.g., 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, or 30). Tolerogenic antigens can be prepared by a number of techniques known in the art, depending on that nature of the molecule. Polynucleotide, polypeptide, and carbohydrate antigens can be isolated from cells of the species to be treated in which they are enriched. Short peptides are conveniently prepared by amino acid synthesis. Longer proteins of known sequence can be prepared by synthesizing an encoding sequence or PCR-amplifying an encoding sequence from a natural source or vector, and then expressing the encoding sequence in a suitable bacterial or eukaryotic host cell. In some embodiments, the antigens are known in the art and are available from commercial government and scientific sources. In some embodiments, the antigens are whole inactivated or attenuated organisms. These organisms may be infectious organisms, such as viruses, parasites and bacteria. These organisms may also be tumor cells. The antigens may be purified or partially purified polypeptides derived from tumors or viral or bacterial sources. Criteria for identifying and selecting effective antigenic peptides (e.g., minimal peptide sequences capable of eliciting an immune response) can be found in the art. The antigens can be recombinant polypeptides produced by expressing DNA encoding the polypeptide antigen in a heterologous expression system. The antigens can be DNA encoding all or part of an antigenic protein. The DNA may be in the form of vector DNA such as plasmid DNA. Antigens may be provided as single antigens or may be provided in combination. Antigens may also be provided as complex mixtures of polypeptides or nucleic acids. In some embodiments, the antigen is a self antigen. As used herein, the term “self- antigen” refers to an immunogenic antigen or epitope which is native to a mammal and which may be involved in the pathogenesis of an autoimmune disease. In some embodiments, the antigen is a viral antigen. Viral antigens can be isolated from any virus including, but not limited to, a virus from any of the following viral families: UM-43148.601 Arenaviridae, Arterivirus, Astroviridae, Baculoviridae, Badnavirus, Barnaviridae, Birnaviridae, Bromoviridae, Bunyaviridae, Caliciviridae, Capillovirus, Carlavirus, Caulimovirus, Circoviridae, Closterovirus, Comoviridae, Coronaviridae (e.g., Coronavirus, such as severe acute respiratory syndrome (SARS) virus), Corticoviridae, Cystoviridae, Deltavirus, Dianthovirus, Enamovirus, Filoviridae (e.g., Marburg virus and Ebola virus (e.g., Zaire, Reston, Ivory Coast, or Sudan strain)), Flaviviridae, (e.g., Hepatitis C virus, Dengue virus 1, Dengue virus 2, Dengue virus 3, and Dengue virus 4), Hepadnaviridae, Herpesviridae (e.g., Human herpesvirus 1, 3, 4, 5, and 6, and Cytomegalovirus), Hypoviridae, Iridoviridae, Leviviridae, Lipothrixviridae, Microviridae, Orthomyxoviridae (e.g., Influenzavirus A and B and C), Papovaviridae, Paramyxoviridae (e.g., measles, mumps, and human respiratory syncytial virus), Parvoviridae, Picornaviridae (e.g., poliovirus, rhinovirus, hepatovirus, and aphthovirus), Poxviridae (e.g., vaccinia and smallpox virus), Reoviridae (e.g., rotavirus), Retroviridae (e.g., lentivirus, such as human immunodeficiency virus (HIV) 1 and HIV 2), Rhabdoviridae (for example, rabies virus, measles virus, respiratory syncytial virus, etc.), Togaviridae (for example, rubella virus, dengue virus, etc.), and Totiviridae. Suitable viral antigens also include all or part of Dengue protein M, Dengue protein E, Dengue D1NS1, Dengue D1NS2, and Dengue D1NS3. Viral antigens may be derived from a particular strain such as a papilloma virus, a herpes virus, i.e. herpes simplex 1 and 2; a hepatitis virus, for example, hepatitis A virus (HAV), hepatitis B virus (HBV), hepatitis C virus (HCV), the delta hepatitis D virus (HDV), hepatitis E virus (HEV) and hepatitis G virus (HGV), the tick-borne encephalitis viruses; parainfluenza, varicella-zoster, cytomeglavirus, Epstein-Barr, rotavirus, rhinovirus, adenovirus, coxsackieviruses, equine encephalitis, Japanese encephalitis, yellow fever, Rift Valley fever, and lymphocytic choriomeningitis. In some embodiments, the antigen is a bacterial antigen. Bacterial antigens can originate from any bacteria including, but not limited to, Actinomyces, Anabaena, Bacillus, Bacteroides, Bdellovibrio, Bordetella, Borrelia, Campylobacter, Caulobacter, Chlamydia, Chlorobium, Chromatium, Clostridium, Corynebacterium, Cytophaga, Deinococcus, Escherichia, Francisella, Halobacterium, Heliobacter, Haemophilus, Hemophilus influenza type B (HIB), Hyphomicrobium, Legionella, Leptspirosis, Listeria, Meningococcus A, B and C, Methanobacterium, Micrococcus, Myobacterium, Mycoplasma, Myxococcus, Neisseria, Nitrobacter, Oscillatoria, Prochloron, Proteus, Pseudomonas, Phodospirillum, Rickettsia, Salmonella, Shigella, Spirillum, Spirochaeta, Staphylococcus, Streptococcus, Streptomyces, Sulfolobus, Thermoplasma, Thiobacillus, and Treponema, Vibrio, and Yersinia. In some embodiments, the antigen is a parasite antigen. Parasite antigens can be obtained UM-43148.601 from parasites such as, but not limited to, an antigen derived from Cryptococcus neoformans, Histoplasma capsulatum, Candida albicans, Candida tropicalis, Nocardia asteroides, Rickettsia ricketsii, Rickettsia typhi, Mycoplasma pneumoniae, Chlamydial psittaci, Chlamydial trachomatis, Plasmodium falciparum, Trypanosoma brucei, Entamoeba histolytica, Toxoplasma gondii, Trichomonas vaginalis and Schistosoma mansoni. These include Sporozoan antigens, Plasmodian antigens, such as all or part of a Circumsporozoite protein, a Sporozoite surface protein, a liver stage antigen, an apical membrane associated protein, or a Merozoite surface protein. In some embodiments, the antigen is an allergen and environmental antigen, such as, but not limited to, an antigen derived from naturally occurring allergens such as pollen allergens (tree-, herb, weed-, and grass pollen allergens), insect allergens (inhalant, saliva and venom allergens), animal hair and dandruff allergens, and food allergens. Important pollen allergens from trees, grasses and herbs originate from the taxonomic orders of Fagales, Oleales, Pinales and platanaceae including i.a. birch (Betula), alder (Alnus), hazel (Corylus), hornbeam (Carpinus) and olive (Olea), cedar (Cryptomeria and Juniperus), Plane tree (Platanus), the order of Poales including i.e. grasses of the genera Lolium, Phleum, Poa, Cynodon, Dactylis, Holcus, Phalaris, Secale, and Sorghum, the orders of Asterales and Urticales including i.a. herbs of the genera Ambrosia, Artemisia, and Parietaria. Other allergen antigens that may be used include allergens from house dust mites of the genus Dermatophagoides and Euroglyphus, storage mite e.g Lepidoglyphys, Glycyphagus and Tyrophagus, those from cockroaches, midges and fleas e.g. Blatella, Periplaneta, Chironomus and Ctenocepphalides, those from mammals such as cat, dog and horse, birds, venom allergens including such originating from stinging or biting insects such as those from the taxonomic order of Hymenoptera including bees (superfamily Apidae), wasps (superfamily Vespidea), and ants (superfamily Formicoidae). Still other allergen antigens that may be used include inhalation allergens from fungi such as from the genera Alternaria and Cladosporium. In some embodiments, the antigen is a tumor antigen. The antigen can be a tumor antigen, including a tumor-associated or tumor-specific antigen, such as, but not limited to, alpha-actinin-4, Bcr-Abl fusion protein, Casp-8, beta-catenin, cdc27, cdk4, cdkn2a, coa-1, dek- can fusion protein, EF2, ETV6-AML1 fusion protein, LDLR-fucosyltransferaseAS fusion protein, HLA-A2, HLA-A11, hsp70-2, KIAAO205, Mart2, Mum-1, 2, and 3, neo-PAP, myosin class I, OS-9, pml-RARα fusion protein, PTPRK, K-ras, N-ras, Triosephosphate isomeras, Bage- 1, Gage 3,4,5,6,7, GnTV, Herv-K-mel, Lage-1, Mage-A1,2,3,4,6,10,12, Mage-C2, NA-88, NY- Eso-1 / Lage-2, SP17, SSX-2, and TRP2-Int2, MelanA (MART-I), gp100 (Pmel 17), tyrosinase, UM-43148.601 TRP-1, TRP-2, MAGE-1, MAGE-3, BAGE, GAGE-1, GAGE-2, p15(58), CEA, RAGE, NY- ESO (LAGS), SCP-1, Hom / Mel-40, PRAME, p53, H-Ras, HER-2 / neu, BCR-ABL, E2A-PRL, H4-RET, IGH-IGK, MYL-RAR, Epstein Barr virus antigens, EBNA, human papillomavirus (HPV) antigens E6 and E7, TSP-180, MAGE-4, MAGE-5, MAGE-6, p185erbB2, p180erbB-3, c-met, nm-23H1, PSA, TAG-72-4, CA 19-9, CA 72-4, CAM 17.1, NuMa, K-ras, β-Catenin, CDK4, Mum-1, p16, TAGE, PSMA, PSCA, CT7, telomerase, 43-9F, 5T4, 791Tgp72, α- fetoprotein, 13HCG, BCA225, BTAA, CA 125, CA 15-3 (CA 27.29\BCAA), CA 195, CA 242, CA-50, CAM43, CD68\KP1, CO-029, FGF-5, G250, Ga733 (EpCAM), human EGFR protein or its fragments, such as human EGFR residues 306–325 (SCVRACGADSYEMEEDGVRK (SEQ ID NO:374)) and residues 897–915 (VWSYGVTVWELMTFGSKPY (SEQ ID NO:375)), HTgp-175, M344, MA-50, MG7-Ag, MOV18, NB\70K, NY-CO-1, RCAS1, SDCCAG16, TA- 90 (Mac-2 binding protein\cyclophilin C-associated protein), TAAL6, TAG72, TLP, TPS, WT1 (and WT1-derivaed peptide sequences: WT1126–134 (RMFP NAPYL (SEQ ID NO:376)), WT1 122–140 (SGQARMFPNAPYLPSCLES (SEQ ID NO:377)), and WT1122–144 (SGQARMFPNAPYLPSCLESQPTI (SEQ ID NO:378)), MUC1 (and MUC1-derived peptides and glycopeptides such as RPAPGS (SEQ ID NO:379), PPAHGVT (SEQ ID NO:380), and PDTRP (SEQ ID NO:381))), LMP2, EGFRvIII, Idiotype, GD2, Ras mutant, p53 mutant, Proteinase3 (PR1), Survivin, hTERT, Sarcoma translocation breakpoints, EphA2, EphA4, LMW-PTP, PAP, ML-IAP, AFP, ERG (TMPRSS2 ETS fusion gene), NA17, PAX3, ALK, Androgen receptor, Cyclin B1, Polysialic acid, MYCN, RhoC, TRP-2, GD3, Fucosyl GM1, Mesothelin, sLe(animal), CYP1B1, PLAC1, GM3, BORIS, Tn, GloboH, NY-BR-1, RGS5, SART3, STn, Carbonic anhydrase IX, PAX5, OY-TES1, Sperm protein 17, LCK, HMWMAA, AKAP-4, XAGE 1, B7H3, Legumain, Tie 2, Page4, VEGFR2, MAD-CT-1, FAP, PDGFR- alpha, PDGFR-β, MAD-CT-2, Fos-related antigen 1, ERBB2, Folate receptor 1 (FOLR1 or FBP), IDH1, IDO, LY6K, fms-related tyro- sine kinase 1 (FLT1, best known as VEGFR1), KDR, PADRE, TA-CIN (recombinant HPV16 L2E7E6), SOX2, and aldehyde dehydrogenase. One of the critical barriers to developing curative and tumor- specific immunotherapy is the identification and selection of highly specific and restricted tumor antigens to avoid autoimmunity. Tumor neo-antigens, which arise as a result of genetic change (e.g., inversions, translocations, deletions, missense mutations, splice site mutations, etc.) within malignant cells, represent the most tumor- specific class of antigens. In some embodiments, the antigen is a neo-antigen. The term neoantigen is used herein to define any newly expressed antigenic determinant. Neoantigens may arise upon conformational change in a protein, as newly expressed determinants (especially on the surfaces UM-43148.601 of transformed or infected cells), as the result of complex formation of one or more molecules or as the result of cleavage of a molecule with a resultant display of new antigenic determinants. Thus, as used herein, the term neoantigen covers antigens expressed upon infection (e.g. viral infection, protozoal infection or bacterial infection), in prion-mediated diseases, an on cell transformation (cancer), in which latter case the neoantigen may be termed a tumour-associated antigen. The present invention is not limited to a particular manner of identifying neo-antigens. In some embodiments, identification of neo-antigens involves identifying all, or nearly all, mutations in the neoplasia / tumor at the DNA level using whole genome sequencing, whole exome (e.g., only captured exons) sequencing, or RNA sequencing of tumor versus matched germline samples from each patient. In some embodiments, identification of neo-antigens involves analyzing the identified mutations with one or more peptide-MHC binding prediction algorithms to generate a plurality of candidate neo-antigen T cell epitopes that are expressed within the neoplasia / tumor and may bind patient HLA alleles. In some embodiments, identification of neo-antigens involves synthesizing the plurality of candidate neo-antigen peptides selected from the sets of all neo open reading frame peptides and predicted binding peptides for use in a cancer vaccine. In some embodiments, the nanoparticles associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) and a peptide antigen are further associated with an adjuvant. Such embodiments are not limited to a particular type of adjuvant. Generally, adjuvants are any substance whose admixture into the vaccine composition increases or otherwise modifies the immune response to the mutant peptide. Carriers are scaffold structures, for example a polypeptide or a polysaccharide, to which the antigenic peptide (e.g., neo-antigenic peptide) is capable of being associated. Optionally, adjuvants are conjugated covalently or non- covalently to the peptides or polypeptides of the invention. The ability of an adjuvant to increase the immune response to an antigen is typically manifested by a significant increase in immune-mediated reaction, or reduction in disease symptoms. For example, an increase in humoral immunity is typically manifested by a significant increase in the titer of antibodies raised to the antigen, and an increase in T-cell activity is typically manifested in increased cell proliferation, or cellular cytotoxicity, or cytokine secretion. An adjuvant may also alter an immune response, for example, by changing a primarily humoral or Th2 response into a primarily cellular, or Thl response. Suitable adjuvants include, but are not limited to 1018 ISS, aluminum salts, Amplivax, UM-43148.601 AS15, BCG, CP-870,893, CpG7909, CyaA, dSLIM, GM-CSF, IC30, IC31, Imiquimod, ImuFact IMP321, IS Patch, ISS, ISCOMATRIX, Juvlmmune, LipoVac, MF59, monophosphoryl lipid A, Montanide IMS 1312, Montanide ISA 206, Montanide ISA 50V, Montanide ISA-51, OK-432, OM-174, OM-197-MP-EC, ONTAK, PepTel.RTM. vector system, PLG microparticles, resiquimod, SRL172, Virosomes and other Virus-like particles, YF-17D, VEGF trap, R848, beta-glucan, Pam3Cys, Aquila's QS21 stimulon (Aquila Biotech, Worcester, Mass., USA) which is derived from saponin, mycobacterial extracts and synthetic bacterial cell wall mimics, and other proprietary adjuvants such as Ribi's Detox. Quil or Superfos. Several immunological adjuvants (e.g., MF59) specific for dendritic cells and their preparation have been described previously (Dupuis M, et al., Cell Immunol.1998; 186(1): 18-27; Allison A C; Dev Biol Stand. 1998; 92:3-11). Also cytokines may be used. Several cytokines have been directly linked to influencing dendritic cell migration to lymphoid tissues (e.g., TNF-alpha), accelerating the maturation of dendritic cells into efficient antigen -presenting cells for T-lymphocytes (e.g., GM- CSF, IL-1 and IL-4) (U.S. Pat. No.5,849,589, specifically incorporated herein by reference in its entirety) and acting as immunoadjuvants (e.g., IL-12) (Gabrilovich D I, et al., J Immunother Emphasis Tumor Immunol.1996 (6):414-418). Toll like receptors (TLRs) may also be used as adjuvants, and are important members of the family of pattern recognition receptors (PRRs) which recognize conserved motifs shared by many micro-organisms, termed "pathogen- associated molecular patterns" (PAMPS). The present invention addresses the need for improved stable and targeted delivery (e.g., in vitro or in vivo) of celastrol (or variants thereof) and / or rapamycin (or variants thereof). Indeed, the present invention addresses such needs through providing synthetic high density lipoprotein (sHDL) nanoparticles for stable and targeted delivery of celastrol (or variants thereof) and / or rapamycin (or variants thereof). Compared to other strategies, including conventional nanoparticle vehicles, sHDL nanoparticles have impressive biocompatibility and capacity for cargo loading. For example, the ultrasmall but tunable size (e.g., 10-20 nm) enables the sHDL nanoparticles to effectively drain to lymph nodes and deliver cargo peptide antigens and nucleic acid-based adjuvants to lymph node-resident dendritic cells, thus positioning them as an efficient platform for co-delivery of antigen and adjuvant for tumor immunotherapy. In certain embodiments, the present invention provides methods for treating, preventing and / or attenuating a disorder comprising administering to a subject (e.g., a human subject UM-43148.601 suffering from or at risk of suffering a disease or medical condition) a composition as described herein. Such methods are not limited to treating a particular disorder. In some embodiments, the disorder is an autoimmune disorder. Such methods are not limited to treating a particular autoimmune disorder. Examples of autoimmune disorders include, but are not limited to, multiple sclerosis (MS), celiac disease, rheumatoid arthritis, primary biliary cholangitis, primary sclerosing cholangitis, MOG antibody disease, diabetes (e.g., type 1 diabetes mellitus), autoimmune diseases of the thyroid (e.g., Hashimoto’s thyroiditis, Graves’ disease), thyroid-associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison’s disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren’s syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi–Goutières syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson’s disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease. In some embodiments, the disorder is a transplantation related disorder. In some embodiments, the disorder is one or more allergies. In some embodiments, the disorder is a respiratory condition (e.g., asthma). In some embodiments, the disorder is graft-versus-host- disease (GvHD). In some embodiments, such methods for treating or preventing autoimmune disorders further comprise co-administering (e.g., simultaneously or at different times) additional therapeutic agents. Examples of such therapeutic agents include, but are not limited to, disease- modifying antirheumatic drugs (e.g., leflunomide, methotrexate, sulfasalazine, hydroxychloroquine), biologic agents (e.g., rituximab, infliximab, etanercept, adalimumab, golimumab), nonsteroidal anti-inflammatory drugs (e.g., ibuprofen, celecoxib, ketoprofen, naproxen, piroxicam, diclofenac), analgesics (e.g., acetaminophen, tramadol), immunomodulators (e.g., anakinra, abatacept), glucocorticoids (e.g., prednisone, methylprednisone), TNF-α inhibitors (e.g., adalimumab, certolizumab pegol, etanercept, golimumab, infliximab), IL-1 inhibitors, and metalloprotease inhibitors. In some embodiments, the therapeutic agents include, but are not limited to, infliximab, adalimumab, etanercept, or UM-43148.601 parenteral gold or oral gold. In some instances, the therapeutic agent is an immunomodulatory agent or immunosuppressant (e.g., statins; mTOR inhibitors, such as rapamycin or a rapamycin analog; TGF-β signaling agents; TGF-β receptor agonists; histone deacetylase inhibitors, such as Trichostatin A; corticosteroids; inhibitors of mitochondrial function, such as rotenone; P38 inhibitors; NF-κβ inhibitors, such as 6Bio, Dexamethasone, TCPA-1, IKK VII; adenosine receptor agonists; prostaglandin E2 agonists (PGE2), such as Misoprostol; phosphodiesterase inhibitors, such as phosphodiesterase 4 inhibitor (PDE4), such as Rolipram; proteasome inhibitors; kinase inhibitors; G-protein coupled receptor agonists; G-protein coupled receptor antagonists; glucocorticoids; retinoids; cytokine inhibitors; cytokine receptor inhibitors; cytokine receptor activators; peroxisome proliferator-activated receptor antagonists; peroxisome proliferator-activated receptor agonists; histone deacetylase inhibitors; calcineurin inhibitors; phosphatase inhibitors; PI3 KB inhibitors, such as TGX-221; autophagy inhibitors, such as 3- Methyladenine; aryl hydrocarbon receptor inhibitors; proteasome inhibitor I (PSI); and oxidized ATPs, such as P2X receptor blockers. Immunosuppressants also include IDO, vitamin D3, cyclosporins, such as cyclosporine A, aryl hydrocarbon receptor inhibitors, resveratrol, azathiopurine (Aza), 6-mercaptopurine (6-MP), 6-thioguanine (6-TG), FK506, sanglifehrin A, salmeterol, mycophenolate mofetil (MMF), aspirin and other COX inhibitors, niflumic acid, estriol, triptolide; OPN-305, OPN-401; Eritoran (E5564); TAK-242; Cpn10; NI-0101; 1A6; AV411; IRS-954 (DV-1079); IMO-3100; CPG-52363; CPG-52364; OPN-305; ATNC05; NI- 0101; IMO-8400; Hydroxychloroquine; CU-CPT22; C29; Ortho-vanillin; SSL3 protein; OPN- 305; 5 SsnB; Vizantin; (+)-N-phenethylnoroxymorphone; VB3323; Monosaccharide 3; (+)- Naltrexone and (+)-naloxone; HT52; HTB2; Compound 4a; CNTO2424; TH1020; INH-ODN; E6446; AT791; CpG ODN 2088; ODN TTAGGG; COV08-0064; 2R9; GpG oligonucleotides; 2-aminopurine; Amlexanox; Bay11-7082; BX795; CH-223191; Chloroquine; CLI-095; CU- CPT9a; Cyclosporin A; CTY387; Gefitnib; Glybenclamide; H-89; H-131; Isoliquiritigenin; MCC950; MRT67307; OxPAPC; Parthenolide; Pepinh-MYD; Pepinh-TRIF; Polymyxin B; R406; RU.521; VX-765; YM201636; Z-VAD-FMK; and AHR-specific ligands; including but not limited to 2,3,7,8-tetrachloro-dibenzo-p-dioxin (TCDD); tryptamine (TA); and 6 formylindolo[3,2 b]carbazole (FICZ)). In particular embodiments, the immunosuppressant is fingolimod; rapamycin; 2-(1’H-indole-3’-carbonyl)-thiazole-4-carboxylic acid methyl ester (ITE) or related ligands; Trichostatin A; and / or Suberoylanilide hydroxamic acid (SAHA). In certain embodiments, the present invention provides methods for treating conditions, disorders and / or diseases with such compositions comprising a nanoparticle (as described herein) (e.g., sHDL associated with celastrol and / or rapamycin). UM-43148.601 The present invention is not limited to specific types of conditions, disorders and / or diseases. In some embodiments, the condition, disorder and / or disease is peripheral ischemia, cancer, an inflammatory disorder, a genetic disorder, etc. In some embodiments, the condition, disorder and / or disease is selected from erythropoietic porphyries, T2 diabetes, antifibrinolytic, central diabetes insipidus, delaying the birth in case of threat of premature birth, antibiotic, cystic fibrosis, angina, anticoagulant in patients with unstable angina undergoing PTCA or PCI, systemic lupus erythematosus, hypercalcemia, osteoporosis, pagets disease, carbetocin works as an oxytocic, antihemorrhagic and uterotonic drug in the peripheral nervous system, prevention of uterine atony, induction, and control postpartum bleeding or haemorrhage, stimulant of the gastric secretion, for treat hormone-sensitive cancers of the prostate and breast, inhibition of premature LH surges in women undergoing controlled ovarian stimulation, immunosuppression in organ transplantation to prevent rejection, peritumoral brain edema, diagnosis of ACTHdependent Cushing’s syndrome, allergies, ankylosing spondylitis, psoriasis, chorioditis, erythema, keratitis, sclerosis, dermatomyositis, rheumatoid arthritis, Stevens-Johnson Syndrome, ulcerative colitis, diagnosis of adrenocortical insufficiency, antibiotic, systemic infections caused by gram positive organisms, nocturnal enuresis, nocturia, and stoppage of bleeding or haemorrhage in haemophilia A patients, acute hereditary angioderma, postmenopausal osteoporosis, anti- parathyroid, Paget’s disease, hypercalcaemia, hypertension, AIDS / HIV-1 infection, acute coronary syndrome, unstable angina undergoing PCI, Alzheimer’s and Parkinson’s disease, inhibition of premature LH surges in women undergoing controlled ovarian hyperstimulation, Relapsing- Remitting Multiple Sclerosis, hepatic insufficiency, wound healing, inflammation of respiratory tract, asthenia, release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary, stimulate the secretion of gonadotropin during disturbances fertility, and diagnosis of the functional capacity and response of the gonadotropes of the anterior pituitary, for skin lesions, surface wounds and eye infections, postmenopausal osteoporosis, Paget’s disease, hypercalcaemia, hereditary angioedema, immune system related diseases, acromegaly, anticoagulant, fibroids and endometriosis, central diabetes insipidus, Cushing’s syndrome, diabetic foot ulcers, treatment of central precocious puberty, uterine fibriods and endometriosis, vasodilatory, natriuretic, diuretic and neurohormonal effects, acromegaly, carcinoid syndrome, acute bacterial skin and skin structure infections, initiation or improvement of uterine contractions, and control postpartum bleeding or haemorrhage, hematide Chronic kidney disease associated anemia, stomatitis, pharyngitis, diagnostic assessment of UM-43148.601 thyroid function, postmenopausal osteoporosis, hypercalcaemia, diagnosis of pancreatic exocrine dysfunction, and gastrinoma, Zollinger-Ellison syndrome, prevention of RDS in premature infants, and meconium aspiration syndrome, acute variceal bleeding, allergic rhinitis and conjunctivitis, spinocerebellar degeneration / ataxia, Short Bowel Syndrome, antibiotic, bactericidal, teriparatide is the only anabolic (i.e., bone growing) agent indicated for use in postmenopausal women with osteoporosis, Cortrosyn Analogue of adrenocorticotrophic hormone (ACTH) used for diagnostic purposes, treatment of adrenal insufficiency, epilepsia, Chronic hepatitis B, chronic hepatitis C, primary and secondary immune deficiencies, acute decompensated heart failure, colitis, esophageal variceal bleeding in patients with cirrhotic liver disease and AIDS-related diarrhea, sarcoidosis and acute lung injury, and severe chronic pain. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having arthritis and / or rheumatoid arthritis, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having leprosy, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having eczema, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having tuberculosis, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having obesity, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having Crohn’s disease, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. UM-43148.601 In some embodiments, the disclosure provides a method for treating a subject having or at risk of having prostate cancer, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for preventing organ transplant rejection, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the disclosure provides a method for treating and / or preventing an inflammatory disorder in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the inflammatory disorder is selected from idiopathic inflammatory diseases or disorders, chronic inflammatory diseases or disorders, acute inflammatory diseases or disorders, autoimmune diseases or disorders, infectious diseases or disorders, inflammatory malignant diseases or disorders, inflammatory transplantation-related diseases or disorders, inflammatory degenerative diseases or disorders, diseases or disorders associated with a hypersensitivity, inflammatory cardiovascular diseases or disorders (e.g., as described herein), inflammatory cerebrovascular diseases or disorders, peripheral vascular diseases or disorders, inflammatory glandular diseases or disorders, inflammatory gastrointestinal diseases or disorders, inflammatory cutaneous diseases or disorders, inflammatory hepatic diseases or disorders, inflammatory neurological diseases or disorders, inflammatory musculo-skeletal diseases or disorders, inflammatory renal diseases or disorders, inflammatory reproductive diseases or disorders, inflammatory systemic diseases or disorders, inflammatory connective tissue diseases or disorders, inflammatory tumors, necrosis, inflammatory implant-related diseases or disorders, inflammatory aging processes, immunodeficiency diseases or disorders, proliferative diseases and disorders, and inflammatory pulmonary diseases or disorders. In some embodiments, the disclosure provides a method for treating a subject having or at risk of having one or more autoimmune disorders, comprising administering to the subject a therapeutically effective amount of a nanoparticle associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. Such methods are not limited to treating a particular type or kind of autoimmune disorder. In some embodiments, the autoimmune disorder is selected from multiple sclerosis UM-43148.601 (MS), celiac disease, rheumatoid arthritis, diabetes (e.g., type 1 diabetes mellitus), autoimmune diseases of the thyroid (e.g., Hashimoto's thyroiditis, Graves' disease), thyroid-associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutières syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease. In some embodiments, the one or more autoimmune disorders is a single autoimmune disorder. In some embodiments, the single autoimmune disorder is celiac disease. In some embodiments, the subject is a human subject. In some embodiments, the method includes administering one more additional therapeutic agents to the subject. In some embodiments, the one or more additional therapeutic agents are administered simultaneously with an effective amount of a composition of any one of the embodiments described herein to the subject. In some embodiments, the one or more additional therapeutic agents are administered at a different time from an effective amount of a composition of any one of the embodiments described herein. In some embodiments, the one or more additional therapeutic agents are selected from the group consisting of corticosteroids, such as prednisone, betamethasone, clobetasone butyrate; and budesonide, immunosuppressants, such as etanercept, adalimumab, azathioprine, infliximab, cyclosporine, alemtuzumab, and cladribine; and anti-inflammatory agents, such as dapsone and sulfonamide. In some embodiments, the one or more additional therapeutic agents are selected from infliximab, adalimumab, etanercept, dapsone or clobetasone butyrate. In some embodiments, the subject adheres to a gluten-free diet. The nanoparticles of the present invention may be characterized for size and uniformity by any suitable analytical techniques. These include, but are not limited to, atomic force microscopy (AFM), electrospray-ionization mass spectroscopy, MALDI-TOF mass spectroscopy, LC-MS / MS,13C nuclear magnetic resonance spectroscopy, high performance liquid chromatography (HPLC), size exclusion chromatography (SEC) (equipped with multi- angle laser light scattering, dual UV and refractive index detectors), capillary electrophoresis, UM-43148.601 and get electrophoresis. These analytical methods assure the uniformity of the sHDL nanoparticle population and are important in the production quality control for eventual use in in vivo applications. In some embodiments, gel permeation chromatography (GPC), which can separate sHDL nanoparticles from liposomes and free ApoA-I mimetic peptide, is used to analyze the sHDL nanoparticles. In some embodiments, the size distribution and zeta-potential are determined by dynamic light scattering (DLS) using, for example, a Malven Nanosizer instrument. Such compositions comprising nanoparticles associated with peptides as described herein are not limited to a particular manner of administering the composition to a subject. Indeed, any acceptable method known to one of ordinary skill in the art may be used to administer such compositions to the subject. The administration may be localized (i.e., to a particular region, physiological system, tissue, organ, or cell type) or systemic. Such compositions can be administered by a number of routes including, but not limited to oral, inhalation (nasal or pulmonary), intravenous, intraperitoneal, intramuscular, transdermal, subcutaneous, topical, subcutaneous, sublingual, or rectal means. Injections can be e.g., intravenous, intradermal, subcutaneous, intramuscular, or intraperitoneal. In some embodiments, the injections can be given at multiple locations. Where clinical applications are contemplated, in some embodiments of the present invention, the compositions comprising nanoparticles associated with peptides as described herein are prepared as part of a pharmaceutical composition in a form appropriate for the intended application. Generally, this entails preparing compositions that are essentially free of pyrogens, as well as other impurities that could be harmful to humans or animals. However, in some embodiments of the present invention, a straight composition comprising nanoparticles associated with peptides as described herein may be administered using one or more of the routes described herein. In preferred embodiments, the compositions are used in conjunction with appropriate salts and buffers to render delivery of the compositions in a stable manner to allow for uptake by target cells. Buffers also are employed when either of the compositions are introduced into a patient. Aqueous compositions comprise an effective amount of the sHDL nanoparticles to cells dispersed in a pharmaceutically acceptable carrier or aqueous medium. Such compositions also are referred to as inocula. The phrase "pharmaceutically or pharmacologically acceptable" refer to molecular entities and compositions that do not produce adverse, allergic, or other untoward reactions UM-43148.601 when administered to an animal or a human. As used herein, "pharmaceutically acceptable carrier" includes any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents and the like. Except insofar as any conventional media or agent is incompatible with the vectors or cells of the present invention, its use in therapeutic compositions is contemplated. Supplementary active ingredients may also be incorporated into the compositions. The active compositions may also be administered parenterally or intraperitoneally or intratumorally. Solutions of the active compounds as free base or pharmacologically acceptable salts are prepared in water suitably mixed with a surfactant, such as hydroxypropylcellulose. Dispersions can also be prepared in glycerol, liquid polyethylene glycols, and mixtures thereof and in oils. Under ordinary conditions of storage and use, these preparations contain a preservative to prevent the growth of microorganisms. The pharmaceutical forms suitable for injectable use include sterile aqueous solutions or dispersions and sterile powders for the extemporaneous preparation of sterile injectable solutions or dispersions. The carrier may be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), suitable mixtures thereof, and vegetable oils. The proper fluidity can be maintained, for example, by the use of a coating, such as lecithin, by the maintenance of the required particle size in the case of dispersion and by the use of surfactants. The prevention of the action of microorganisms can be brought about by various antibacterial an antifungal agents, for example, parabens, chlorobutanol, phenol, sorbic acid, thimerosal, and the like. In many cases, it may be preferable to include isotonic agents, for example, sugars or sodium chloride. Prolonged absorption of the injectable compositions can be brought about by the use in the compositions of agents delaying absorption, for example, aluminum monostearate and gelatin. Sterile injectable solutions are prepared by incorporating either of the compositions in the required amount in the appropriate solvent with various of the other ingredients enumerated above, as required, followed by filtered sterilization. Generally, dispersions are prepared by incorporating the various sterilized active ingredients into a sterile vehicle which contains the basic dispersion medium and the required other ingredients from those enumerated above. In the case of sterile powders for the preparation of sterile injectable solutions, the preferred methods of preparation are vacuum-drying and freeze-drying techniques which yield a powder of the active ingredient plus any additional desired ingredient from a previously sterile-filtered solution thereof. UM-43148.601 Upon formulation, either of the compositions are administered in a manner compatible with the dosage formulation and in such amount as is therapeutically effective. The formulations are easily administered in a variety of dosage forms such as injectable solutions, drug release capsules and the like. For parenteral administration in an aqueous solution, for example, the solution is suitably buffered, if necessary, and the liquid diluent first rendered isotonic with sufficient saline or glucose. These particular aqueous solutions are especially suitable for intravenous, intramuscular, subcutaneous, and intraperitoneal administration. For example, one dosage could be dissolved in 1 ml of isotonic NaCl solution and either added to 1000 ml of hypodermoclysis fluid or injected at the proposed site of infusion, (see for example, "Remington's Pharmaceutical Sciences" 15th Edition, pages 1035-1038 and 1570-1580). In some embodiments of the present invention, the active particles or agents are formulated within a therapeutic mixture to comprise about 0.0001 to 1.0 milligrams, or about 0.001 to 0.1 milligrams, or about 0.1 to 1.0 or even about 10 milligrams per dose or so. Multiple doses may be administered. Additional formulations that are suitable for other modes of administration include vaginal suppositories and pessaries. A rectal pessary or suppository may also be used. Suppositories are solid dosage forms of various weights and shapes, usually medicated, for insertion into the rectum, vagina, or the urethra. After insertion, suppositories soften, melt or dissolve in the cavity fluids. In general, for suppositories, traditional binders and carriers may include, for example, polyalkylene glycols or triglycerides; such suppositories may be formed from mixtures containing the active ingredient in the range of 0.5% to 10%, preferably 1%-2%. Vaginal suppositories or pessaries are usually globular or oviform and weighing about 5 g each. Vaginal medications are available in a variety of physical forms, e.g., creams, gels, or liquids, which depart from the classical concept of suppositories. The compositions also may be formulated as inhalants. In some embodiments, the present invention also provides kits comprising a composition comprising one or more nanoparticles associated with celastrol (or variants thereof) and / or rapamycin (or variants thereof) as described herein. In some embodiments, the kits comprise one or more of the reagents and tools necessary to generate either composition, and methods of using either of such compositions. In certain embodiments, the nanoparticles as described herein (e.g., configured for RNA Interference) (e.g., configured for activating an immune response) are further associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) one or more UM-43148.601 therapeutic agents. Such embodiments are not limited to particular type or kind of therapeutic agent. In some embodiments, the therapeutic agent configured for treating and / or preventing cancer. Examples of such therapeutic agents include, but are not limited to, chemotherapeutic agents, anti-oncogenic agents, anti-angiogenic agents, tumor suppressor agents, anti-microbial agents, etc. In some embodiments, the therapeutic agent is configured for treating and / or preventing autoimmune disorders and / or inflammatory disorders. Examples of such therapeutic agents include, but are not limited to, disease-modifying antirheumatic drugs (e.g., leflunomide, methotrexate, sulfasalazine, hydroxychloroquine), biologic agents (e.g., rituximab, infliximab, etanercept, adalimumab, golimumab), nonsteroidal anti-inflammatory drugs (e.g., ibuprofen, celecoxib, ketoprofen, naproxen, piroxicam, diclofenac), analgesics (e.g., acetaminophen, tramadol), immunomodulators (e.g., anakinra, abatacept), glucocorticoids (e.g., prednisone, methylprednisone), TNF-α inhibitors (e.g., adalimumab, certolizumab pegol, etanercept, golimumab, infliximab), IL-1 inhibitors, and metalloprotease inhibitors. In some embodiments, the therapeutic agents include, but are not limited to, infliximab, adalimumab, etanercept, parenteral gold or oral gold. In some embodiments, the therapeutic agent is configured for treating and / or preventing cardiovascular related disorders (e.g., atherosclerosis, heart failure, arrhythmia, atrial fibrillation, hypertension, coronary artery disease, angina pectoris, etc.). Examples of therapeutic agents known to be useful in treating and / or preventing cardiovascular related disorders include, angiotensin-converting enzyme (ACE) inhibitors (e.g., benazepril, enalapril, Lisinopril, perindopril, Ramipril), adenosine, alpha blockers (alpha adrenergic antagonist medications) (e.g., clonidine, guanabenz, labetalol, phenoxybenzamine, terazosin, doxazosin, guanfacine, methyldopa, prazosin), angtiotensin II receptor blockers (ARBs) (e.g., candesartan, irbesartan, olmesartan medoxomil, telmisartan, eprosartan, losartan, tasosartan, valsartan), antiocoagulants (e.g., heparin fondaparinux, warfarin, ardeparin, enoxaparin, reviparin, dalteparin, nadroparin, tinzaparin), antiplatelet agents (e.g., abciximab, clopidogrel, eptifibatide, ticlopidine, cilostazol, dipyridamole, sulfinpyrazone, tirofiban), beta blockers (e.g., acebutolol, betaxolol, carteolol, metoprolol, penbutolol, propranolol, atenolol, bisoprolol, esmolol, nadolol, pindolol, timolol), calcium channel blockers (e.g., amlopidine, felodipine, isradipine, nifedipine, verapamil, diltiazem, nicardipine, nimodipine, nisoldipine), diuretics, aldosterone blockers, loop diuretics (e.g., bumetanide, furosemide, ethacrynic acid, torsemide), potassium-sparing diuretics, thiazide diuretics (e.g., chlorothiazide, chlorthalidone, hydrochlorothiazide, hydroflumethiazide, UM-43148.601 methyclothiazide, metolazone, polythiazide, quinethazone, trichlormethiazide), inoptropics, bile acid sequestrants (e.g., cholestyramine, coletipol, colesevelam), fibrates (e.g., clofibrate, gemfibrozil, fenofibrate), statins (e.g., atorvastatinm, lovastatin, simvastatin, fluvastatin, pravastatin), selective cholesterol absorption inhibitors (e.g., ezetimibe), potassium channel blockers (e.g., amidarone, ibutilide, dofetilide), sodium channel blockers (e.g., disopyramide, mexiletine, procainamide, quinidine, flecainide, moricizine, propafenone), thrombolytic agents (e.g., alteplase, reteplase, tenecteplase, anistreplase, streptokinase, urokinase), vasoconstrictors, vasodilators (e.g., hydralazine, minoxidil, mecamylamine, isorbide dintrate, isorbide mononitrate, nitroglycerin). In some embodiments, the nanoparticles are further associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) agents useful for determining the location of administered particles. Agents useful for this purpose include fluorescent tags, radionuclides and contrast agents. Suitable imaging agents include, but are not limited to, fluorescent molecules such as those described by Molecular Probes (Handbook of fluorescent probes and research products), such as Rhodamine, fluorescein, Texas red, Acridine Orange, Alexa Fluor (various), Allophycocyanin, 7-aminoactinomycin D, BOBO-1, BODIPY (various), Calcien, Calcium Crimson, Calcium green, Calcium Orange, 6-carboxyrhodamine 6G, Cascade blue, Cascade yellow, DAPI, DiA, DID, Di1, DiO, DiR, ELF 97, Eosin, ER Tracker Blue-White, EthD-1, Ethidium bromide, Fluo-3, Fluo4, FM1-43, FM4-64, Fura-2, Fura Red, Hoechst 33258, Hoechst 33342, 7-hydroxy-4-methylcoumarin, Indo-1, JC-1, JC-9, JOE dye, Lissamine rhodamine B, Lucifer Yellow CH, LysoSensor Blue DND-167, LysoSensor Green, LysoSensor Yellow / Blu, Lysotracker Green FM, Magnesium Green, Marina Blue, Mitotracker Green FM, Mitotracker Orange CMTMRos, MitoTracker Red CMXRos, Monobromobimane, NBD amines, NeruoTrace 500 / 525 green, Nile red, Oregon Green, Pacific Blue. POP-1, Propidium iodide, Rhodamine 110, Rhodamine Red, R-Phycoerythrin, Resorfin, RH414, Rhod-2, Rhodamine Green, Rhodamine 123, ROX dye, Sodium Green, SYTO blue (various), SYTO green (Various), SYTO orange (various), SYTOX blue, SYTOX green, SYTOX orange, Tetramethylrhodamine B, TOT-1, TOT-3, X-rhod-1, YOYO-1, YOYO-3. In some embodiments, ceramides are provided as imaging agents. In some embodiments, S1P agonists are provided as imaging agents. Additionally radionuclides can be used as imaging agents. Suitable radionuclides include, but are not limited to radioactive species of Fe(III), Fe(II), Cu(II), Mg(II), Ca(II), and Zn(I1) Indium, Gallium and Technetium. Other suitable contrast agents include metal ions generally used for chelation in paramagnetic T1-type MIR contrast agents, and include di- and UM-43148.601 tri-valent cations such as copper, chromium, iron, gadolinium, manganese, erbium, europium, dysprosium and holmium. Metal ions that can be chelated and used for radionuclide imaging, include, but are not limited to metals such as gallium, germanium, cobalt, calcium, indium, iridium, rubidium, yttrium, ruthenium, yttrium, technetium, rhenium, platinum, thallium and samarium. Additionally metal ions known to be useful in neutron-capture radiation therapy include boron and other metals with large nuclear cross-sections. Also suitable are metal ions useful in ultrasound contrast, and X-ray contrast compositions. Examples of other suitable contrast agents include gases or gas emitting compounds, which are radioopaque. In some embodiments, the nanoparticles are further associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) a targeting agent. For example, in some embodiments wherein the nanoparticle is a sHDL nanoparticle, targeting agents are used to assist in delivery of the sHDL-celastrol or sHDL-rapamycin nanoparticles to desired body regions. Examples of targeting agents include, but are not limited to, an antibody, receptor ligand, hormone, vitamin, and antigen, however, the present invention is not limited by the nature of the targeting agent. In some embodiments, the antibody is specific for a disease- specific antigen. In some embodiments, the receptor ligand includes, but is not limited to, a ligand for CFTR, EGFR, estrogen receptor, FGR2, folate receptor, IL-2 receptor, glycoprotein, and VEGFR. In some embodiments, the receptor ligand is folic acid. In some embodiments, the nanoparticles (e.g., sHDL nanoparticles) of the present invention may be delivered to local sites in a patient by a medical device. Medical devices that are suitable for use in the present invention include known devices for the localized delivery of therapeutic agents. Such devices include, but are not limited to, catheters such as injection catheters, balloon catheters, double balloon catheters, microporous balloon catheters, channel balloon catheters, infusion catheters, perfusion catheters, etc., which are, for example, coated with the therapeutic agents or through which the agents are administered; needle injection devices such as hypodermic needles and needle injection catheters; needleless injection devices such as jet injectors; coated stents, bifurcated stents, vascular grafts, stent grafts, etc.; and coated vaso-occlusive devices such as wire coils. Exemplary devices are described in U.S. Pat. Nos.5,935,114; 5,908,413; 5,792,105; 5,693,014; 5,674,192; 5,876,445; 5,913,894; 5,868,719; 5,851,228; 5,843,089; 5,800,519; 5,800,508; 5,800,391; 5,354,308; 5,755,722; 5,733,303; 5,866,561; 5,857,998; 5,843,003; and 5,933,145; the entire contents of which are incorporated herein by reference. Exemplary stents that are commercially available and may be used in the present application include the RADIUS UM-43148.601 (SCIMED LIFE SYSTEMS, Inc.), the SYMPHONY (Boston Scientific Corporation), the Wallstent (Schneider Inc.), the PRECEDENT II (Boston Scientific Corporation) and the NIR (Medinol Inc.). Such devices are delivered to and / or implanted at target locations within the body by known techniques. In some embodiments, the present invention also provides kits comprising nanoparticles (e.g., sHDL nanoparticles) associated with celastrol and / or rapamcyin as described herein. In some embodiments, the kits comprise one or more of the reagents and tools necessary to generate sHDL nanoparticles associated with celastrol and / or rapamcyin, and methods of using such sHDL nanoparticles associated with celastrol and / or rapamcyin. EXAMPLES The following example is provided in order to demonstrate and further illustrate certain preferred embodiments and aspects of the present invention and are not to be construed as limiting the scope thereof. Use of pronouns such as, “we”, “our,” and “I” refer to the inventive entity. Example 1. This example demonstrates formulation and characterization of Celastrol-DMPC sHDL nanoparticles. Figure 1A illustrates celastrol-DMPC sHDL nanoparticles exhibited clear, orange-tinted appearance following aqueous reconstitution in the absence of visible aggregates. Figure 1B shows that celastrol-DMPC sHDL nanoparticle size via DLS demonstrated a narrowly distributed size range (average diameter 10-12 nm) after 0.22 micron filtration and centrifugal ultrafiltration, suggesting uniform particle sizes conducive to consistent drug delivery. Figure 1C and 1D illustrate loading of celastrol in sHDL and confirmation of celastrol drug loading after methanol disruption of nanoparticle assembly via an analytical biphenyl RP-HPLC for separation of nanoparticle components. Absorbance at 220 nm (top chromatogram) demonstrates successful separation of 22A (scaffolding peptide), celastrol and DMPC (phospholipid). Absorbance at 424 nm (bottom chromatogram) shows absorption peak of celastrol used for quantitation. Figure 1E demonstrates relative stability of the formulation stored at 4 ^C via over a 107 day period with polydispersity index less than 0.3. Example 2. UM-43148.601 This example demonstrates formulation and characterization of Celastrol-DPPC sHDL nanoparticles. Figure 2A illustrates celastrol-DPPC sHDL nanoparticles exhibited clear, orange-tinted appearance after aqueous reconstitution in the absence of visible aggregates. Figure 2B shows that celastrol-DPPC sHDL nanoparticle size via DLS demonstrated a narrowly distributed size range (average diameter 9-10 nm) after filtration and centrifugal ultrafiltration, suggesting uniform particle sizes conducive to consistent drug delivery. Figure 2C illustrates confirmation of celastrol drug loading after methanol disruption of nanoparticle assembly via an analytical biphenyl RP-HPLC for separation of nanoparticle components. Absorbance at 220 nm (top chromatogram) demonstrates successful separation of 22A (scaffolding peptide), celastrol and DPPC (phospholipid). Absorbance at 424 nm (bottom chromatogram) shows absorption peak of celastrol used for quantitation. Example 3. This example demonstrates quantification of Celastrol loading in DMPC sHDL nanoparticles via UV-VIS spectroscopy. Figure 3A-B illustrates the UV-VIS spectrum of Celastrol standards solubilized in DMSO. The graph shows absorbance across the wavelength range of 200 nm to 600 nm, highlighting the characteristic peaks of Celastrol used for generation of a standard curve. Figure 3C demonstrates the UV-VIS spectrum of a diluted sample of Celastrol-loaded DMPC sHDL nanoparticles. Peak absorbance at 424 nm is used to quantify Celastrol concentration in the nanoparticles following disruption by DMSO. Example 4. This example demonstrates the effects of Celastrol on RAW 264.7 macrophage cell line stimulation response. Figure 4A illustrates the celastrol-DMPC sHDL nanoparticle and free celastrol (DMSO) dose-response curve. The results show that celastrol decreases nitrite production in LPS- stimulated RAW 264.7 cells with no loss of bioactivity when celastrol is encapsulated sHDL nanoparticles. Figure 4B is a bar graph depicting IL-6 cytokine levels in the cell culture supernatant after treatment with different concentrations of Celastrol either as a free compound or encapsulated into sHDL nanoparticles. This panel demonstrates the anti-inflammatory potential of Celastrol with near abolishment of IL-6 production in a dose responsive manner. Figure 4C shows the levels of TNF-α cytokine after Celastrol treatment, demonstrating a UM-43148.601 significant dose-dependent inhibition of TNF-α. Figure 4D illustrates an MTS toxicity assay, showing cell viability across a range of celastrol concentrations. This panel assesses the cytotoxicity of celastrol, comparing its effects in a free form or sHDL nanoparticle form. The results show similar cytotoxicity of celastrol in a free form or nanoparticle form. Example 5. This example demonstrates inhibition of NF-κB activation by Celastrol in THP-1 NF-κB reporter cell line and cytotoxicity assessment. Figure 5A displays a dose-response curve for Celastrol-DMPC sHDL nanoparticles or free Celastrol (DMSO) in THP-1 cells stimulated with LPS (50 ng / mL). The graph measures optical density (OD) at 640 nm as a surrogate for NF-κB activity using a QUANTI-Blue reporter-based assay. Figure 5B illustrates controls used in the experiments, including PBS, 0.01% DMSO, and blank DMPC sHDL nanoparticles. These controls establish the baseline responses to ensure that observed effects in Figure 5A are specific to Celastrol's bioactivity and not due to other components of the experimental setup. Figure 5C provides the calculated IC50 values, demonstrating the concentration of Celastrol required to inhibit 50% of NF-κB activity. This curve is plotted for both Celastrol-DMPC sHDL nanoparticles and free Celastrol, highlighting a significantly increased potency of the celastrol-DMPC nanoparticle relative to free celastrol. Figure 5D shows the cytotoxicity of free celastrol, celastrol-DMPC sHDL nanoparticles, and relevant controls. Notably no significant cytotoxic effects were observed at celastrol concentrations below 1000 nM, demonstrating a wide therapeutic index and efficacy. Example 6. This example demonstrates the effects of Celastrol-DMPC sHDL nanoparticles on inflammatory responses in human fibroblast-like synoviocytes (FLS). Figure 6A demonstrates the dose-response effects of celastrol-DMPC sHDL nanoparticles on cytokine and chemokine production after stimulation with IL-1β (10 ng / mL). The bar graphs display the concentration-dependent inhibition of IL-6, IL-8, and MCP-1 production in FLS cultures. The results indicate a robust suppression of these inflammatory cytokines, particularly highlighting the dramatic reduction of IL-6 and other chemokines. Figure 6B displays the dose-response effects on cytokine and chemokine production when FLS cells are stimulated with TNF-α (10 ng / mL). Unlike the response to IL-1β, TNF-α-induced cytokine production is less dramatically inhibited by celastrol-nanodiscs. This suggests different UM-43148.601 underlying mechanisms in the cellular response to TNF-α, which may not involve the same pathways as those modulated by IL-1β. Example 7. This example provides the materials and methods pertaining to Examples 1-6. Celastrol-DMPC sHDL Nanoparticle Formulation: Celastrol, sHDL peptide (22A), and 1,2- Dimyristoyl-sn-glycero-3-phosphocholine (DMPC) phospholipids in a 0.26 / 1 / 2 ratio (w / w) were solubilized in glacial acetic acid, flash frozen in liquid nitrogen, lyophilized overnight and re- hydrated in 10 mM phosphate buffer (pH 7.4) with three 5 minute cycles of heating / cooling at 40°C / 4°C. Resulting solution was filtered with 0.22 micron filter and buffer exchanged with 3 volumes of phosphate buffer via ultracentrifugation using Millipore Ultracentrifugation Filters (MWCO 50k) to remove unbound drug for encapsulation efficiency calculations as discussed below. Characterization of Celastrol-DMPC sHDL Nanoparticles: Celastrol-DMPC sHDL nanoparticles were analyzed via dynamic light scattering following a 1:10 dilution in 10 mM phosphate buffer (pH 7.4) before measurement of average size and distribution on a Malvern Zetasizer Nano (Fig.1A). Long-term DLS measurements to assess nanoparticle stability were performed over a 107 day period (Fig.1E). After filtration and buffer exchange, drug encapsulation efficiency and celastrol quantification were performed via reversed phase high- performance (RP-HPLC) chromatography. Samples were prepared by dissolving 50 µL of celastrol-DMPC sHDL nanoparticle with 50 µL of methanol and filtered through a 0.22 µm syringe filter to remove particulate matter and a 10 µL injection on a 5 micron Phenomenex Biphenyl analytical column. The method utilized mobile phases of solvent A (water with 0.05% trifluoroacetic acid) and solvent B (50:50 water / methanol with 0.05% trifluoroacetic acid) with starting conditions of 30% Solvent B, linearly increased to 100% over 60 minutes. The flow rate was maintained at 0.7 mL / min, and the column temperature was set at 25°C. Detection was carried out using a UV detector set at 220 and 424 nm. Celastrol loading concentration was determined using celastrol standards prepared separately in methanol for generation of a standard curve. Ultraviolet-visible spectrum measurements for celastrol quantification: Celastrol standards were prepared in DMSO and read in a quartz cuvette from 200 nm – 600 nm in 5 nm increments on a UM-43148.601 SpectraMax Multi-Mode microplate reader. Absorbance at 424 nm was used to plot a standard curve. DMSO mediated celastrol-DMPC sHDL nanoparticle assembly disruption was performed. Celastrol quantification was performed using peak absorbance at 424 nm. RAW 264.7 cell culture: Cell lines were purchased from ATCC and cultured in DMEM media supplemented with 10% FBS and 1% pen / strep and plated in 96 well tissue culture plates and grown to 80-90% confluence. Cells were pre-incubated with drug or vehicle 1 hour prior to stimulation with LPS (1 µg / mL) for 24 hours. Supernatants were analyzed for quantification of nitrate via Griess assay (Abcam #ab234044) and cytokine measurements via ELISA at University of Michigan Immunology Core. THP-1 NF-κB Reporter Monocyte cell culture: Cell lines were obtained from InvivoGen and cultured in RPMI 1640, 10% FBS and 1% pen / strep and plated in 96 well tissue culture plates. Cells were pre-incubated with drug or vehicle 1 hour prior to stimulation with LPS (50 ng / mL) for 24 hours. Supernatant was collected for quantification of secreted embryonic alkaline phosphatase (SEAP) via addition of QUANTI-blue as reporter for NF-κB. OD was read at 640 nm and data normalized for NF-κB inhibition plots. Fibroblast like synoviocyte cell culture: Approach utilized previously isolated human FLS cells between passages 3-8. FLS were grown in RPMI supplemented with 10% FBS and 1% pen / strep, pre-incubated for 1 hour with varying concentrations of celastrol-DMPC sHDL nanoparticles and then stimulated with TNFα (10 ng / mL) or IL-1 (10 ng / mL) for 12-24 hours. Determination of the effects of celastrol-DMPC sHDL nanoparticles on relevant cytokines (IL- 1β, IL-6, TNF-α) and chemokines (MCP-1, IL-8) was performed via ELISA by the University of Michigan Immunology Core Facility. MTS Cell Viability Assessment: RAW 264.7, THP-1 and FLS cells were plated into 96-well plates with culture conditions and treatments as described above. Post-treatment, 20 µL of MTS reagent (MTS Assay Kit, Abcam) was added to each well. Cells were incubated for 1-4 hours at 37°C, allowing the MTS tetrazolium compound to be metabolized by viable cells into a colored formazan product. The absorbance of the formazan product was measured at 490 nm using a microplate reader. UM-43148.601 Data Analysis: Data were plotted as mean ± standard deviation (SD) of triplicates from at least three independent experiments. Statistical analysis was performed using one-way ANOVA followed by a post-hoc test for multiple comparisons where appropriate using Graphpad Prism software. Statistical significance is indicated as follows: * denotes p < 0.05, ** denotes p < 0.01, and *** denotes p < 0.001. Example 8. This example investigated whether pre-treatment of mice with celastrol-sHDL nanoparticles can reduce joint swelling in the zymosan-induced arthritis (ZIA) model. Figure 7A shows schematic representation of the experimental design for the ZIA model. Mice were pre-treated with PBS or celastrol-loaded DMPC sHDL nanoparticles (1 mg / kg celastrol) prior to intra-articular injection of zymosan. Joint swelling was assessed by measuring the change in medial-to-lateral joint diameter (Fig.7B). Mice pre-treated with Cel-DMPC sHDL nanoparticles exhibited significantly reduced joint swelling compared to PBS-treated controls. Data are presented as mean ± SEM; ** denotes p < 0.01 by unpaired t-test. Overall, these results that pre-treatment of mice with celastrol-sHDL nanoparticles can reduce joint swelling in the zymosan-induced arthritis (ZIA) model. Next, whether Celastrol-sHDL nanoparticles can also exert beneficial effects in the collagen-induced arthritis (CIA) model was examined. Figure 8A shows a schematic representation of the CIA experimental setup. Mice were immunized with type II collagen emulsified in complete Freund's adjuvant (CFA) on Day 0 and boosted with type II collagen in incomplete Freund's adjuvant (IFA) on Day 21. Upon clinical arthritis onset (Day 25–31), mice were treated with celastrol-loaded nanodiscs (1 mg / kg celastrol) every other day. Arthritis severity was assessed every other day using a composite clinical arthritis score (see, Fig.8B). Therapeutic administration of Celasterol-sHDL nanoparticles significantly reduced disease severity. Data are shown as mean ± SEM, **** denotes p < 0.0001 by two-way ANOVA with Tukey’s post-hoc test. Taken together, these examples demonstrate the therapeutic potential of Celastrol-sHDL nanoparticles in the collagen-induced arthritis (CIA) model as well as the zymosan-induced arthritis (ZIA) model. The following materials and methods pertain to the experiments recited in Example 8. Zymosan-induced arthritis model. Male C57BL / 6 mice (6–8 weeks old) were used to induce acute arthritis via intra-articular injection of zymosan. Zymosan was solubilized in PBS at 30 UM-43148.601 mg / mL and heated at 99ºC with shaking at 1000 RPM and sonicated. Mice were pre-treated via intraperitoneal injection with Celastrol-DMPC sHDL 1 mg / kg or vehicle (PBS) at -2 hours. Mice were anesthetized using isoflurane and administered a single intra-articular injection of prepared zymosan stock solution (10 μL). Mice were pre-treated via intraperitoneal injection with Celastrol-DMPC sHDL 1 mg / kg or vehicle (PBS) at -2 hours. Joint swelling was assessed 48 hours after zymosan challenge by measuring medial-to-lateral joint diameter using digital calipers. Collagen-induced arthritis model. Male DBA / 1 mice (6–8 weeks old) were used to induce collagen-induced arthritis (CIA). On Day 0, mice were immunized via intradermal injection at the base of the tail with 100 μg of bovine type II collagen emulsified in complete Freund’s adjuvant (CFA; 1:1 ratio, total volume 100 μL). On Day 21, mice received a booster injection of 100 μg of type II collagen emulsified in incomplete Freund’s adjuvant (IFA) at different location. Mice were monitored daily for the onset of arthritis beginning on Day 25, with clinical signs defined by swelling and / or erythema in at least one paw. Upon arthritis onset (typically Days 25–31), mice were randomized and treated via intraperitoneal injection with either celastrol- DMPC sHDL nanoparticles (1 mg / kg) or PBS vehicle. Arthritis severity was scored daily using a composite clinical scoring system (0–4 per paw). Example 9. This example demonstrates synthesis and characterization of sHDL nanoparticles carrying rapamycin and antigen peptides. Regulatory T cell (Treg)-inducing effects in a bone marrow-derived dendritic cell (BMDC) and CD4+ T cell coculture study in vitro as well as in vivo in an adoptive cell transfer study were additionally examined. Figure 9A illustrates the loading sequence of sHDL nanoparticles with antigen peptides and rapamycin. Figure 9B shows that rapamycin-antigen-DMPC sHDL nanoparticle size via DLS demonstrated a narrowly distributed size range (7-10 nm) after 0.22 micron filtration and centrifugal ultrafiltration, suggesting uniform particle sizes conducive to consistent drug delivery. Figure 10 shows stacked chromatograms illustrating confirmation of antigen and rapamycin drug loading after methanol disruption of nanoparticle assembly via an analytical biphenyl RP-HPLC for separation of nanoparticle components. The bottommost chromatogram demonstrates successful separation of 22A (scaffolding peptide), rapamycin, antigen-lipid UM-43148.601 conjugate, and DMPC (phospholipid) at 220 nm absorbance. Upper chromatograms are representative chromatograms of standards for each component. To assess the effect of rapamycin-antigen-sHDL nanoparticles on Treg cell induction in vitro, BMDCs were treated with nanoparticles loaded with rapamycin and OVA323-339 (OVA- II) peptide for 24 hours and cocultured with CD4+ T cells from OT-II transgenic mice under Treg-inducing conditions for 5 days (Figure 11A). BMDCs were treated with OVA-II peptide with or without rapamycin at increasing concentrations of 5, 50, 500 ng / mL and 1, 10, 100 ng / mL, respectively (Figure 11B). Treatment of OVA-II peptide alone in both free or nanoparticle-loaded forms did not induce expansion of Treg cells compared to the PBS-treated control group. However, the additional treatment of rapamycin resulted in dose-dependent increases in the frequencies of CD25+Foxp3+ Tregs among CD4+ T cells for both free or nanoparticle-loaded forms. The results show that co-treatment of rapamycin and antigen-peptide enhance Treg induction in a dose-dependent manner that is irrespective of free or nanoparticle forms in vitro. To assess the effect of rapamycin-antigen-sHDL nanoparticles on antigen-specific Treg induction in vivo, OT-II+Thy1.1+CD4+ T cells were adoptively transferred to naïve C57BL / 6 mice, followed by administration of nanoparticles loaded with 13 ug rapamycin and 100 ug OVA-II peptide 1 day after the transfer and analysis of peripheral blood mononuclear cells (PBMCs) 5 days after the nanoparticle administration (Figure 12A). By the time of PBMC analysis, PBS and free OVA-II peptide groups had nearly depleted levels of donor OT- II+Thy1.1+CD4+ T cells, whereas mice that received nanoparticles loaded with OVA-II peptide had significantly higher levels (Figure 12B, left). Interestingly, the codelivery of rapamycin and OVA-II peptide in nanoparticle form resulted in a 2-fold increase in donor T cell frequencies. As expansion of CD4+ T cells is consequent of TCR recognition of MHC class II presented peptides, the results suggest that the nanoparticles effectively deliver antigen peptides and enhance antigen presentation to CD4+ T cells, and that this effect is amplified upon co-delivery of rapamycin. The same trend is seen in CD25+Foxp3+ donor Treg cells (Figure 12B, right). The results suggest that delivery of antigen peptide with nanoparticles alone can induce tolerogenic T cell priming, which is significantly enhanced upon co-delivery of rapamycin. The following materials and methods pertain to the experiments recited in Example 8. Rapamycin-Antigen-sHDL Nanoparticle Formulation: sHDL peptide (22A) and 1,2- Dimyristoyl-sn-glycero-3-phosphocholine (DMPC) phospholipids in a 1 / 2 ratio (w / w) were solubilized in glacial acetic acid, flash frozen in liquid nitrogen, lyophilized overnight and re- UM-43148.601 hydrated in 10 mM phosphate buffer (pH 7.4) with three 5 minute cycles of heating / cooling at 50°C / 4°C. Lipid-peptide conjugates were prepared by dissolving 1,2-Dioleoyl-sn-glycero-3- phosphoethanolamine (DOPE)-maleimide and cysteine-terminated antigen peptides in DMSO and mixing overnight. Lipid-peptide conjugates were added dropwise to pre-formed sHDL nanoparticles and gently mixed for 30 minutes at room temperature. For the loading of rapamycin, the drug was dissolved in DMSO, added dropwise to sHDL nanoparticles at a 0.04 / 1 / 2 rapamycin / 22A / DMPC ratio (w / w), and gently mixed for 30 minutes at room temperature. The resulting solution was filtered with 0.22 micron filter and buffer exchanged with 3 volumes of phosphate buffer via ultracentrifugation using Millipore Ultracentrifugation Filters (MWCO 30k) to remove unbound drug and peptide for encapsulation efficiency calculations as discussed below. Characterization of Particle Size Distribution of Rapamcyin-Antigen-sHDL Nanoparticles: Rapamycin-antigen-sHDL nanoparticles were analyzed via dynamic light scattering by measurement of average size and distribution on a Malvern Zetasizer Nano (Fig.9B). Characterization of Drug and Peptide-loading of Rapamcyin-Antigen-sHDL Nanoparticles: Rapamycin drug and peptide encapsulation efficiency and rapamycin quantification were performed via reversed phase high-performance (RP-HPLC) chromatography (Fig.10). Samples were prepared by dissolving 50 µL of rapamycin-DMPC sHDL nanoparticle with 150 µL of methanol and filtered through a 0.22 µm syringe filter to remove particulate matter and a 10 µL injection on a 5 micron Phenomenex Biphenyl analytical column. The method utilized mobile phases of solvent A (water with 0.05% trifluoroacetic acid) and solvent B (50:50 water / methanol with 0.05% trifluoroacetic acid) with starting conditions of 30% Solvent B, linearly increased to 100% over 60 minutes. The flow rate was maintained at 0.7 mL / min, and the column temperature was set at 25°C. Detection was carried out using a UV detector set at 220 and 280 nm. Encapsulation efficiencies and loading concentrations were determined using lipid-peptide conjugate and rapamycin standards prepared separately in methanol for generation of standard curves. BMDC and CD4+ T cell coculture: To prepare BMDCs, bone-marrow cells were isolated from C57BL / 6 mice and cultured in RPMI media supplemented with 10% FBS, 100 U / mL penicillin, 100 μg / ml streptomycin, 50 μM β-mercaptoethanol, and 20 ng / ml GM-CSF for 7 days. BMDCs were plated in flat-bottom 96 well tissue culture plates overnight, followed by incubation with UM-43148.601 peptide, drug, or nanoparticles for 24 hours. CD4+ T cells were isolated using EasySep™ Mouse CD4+ T Cell Isolation Kit (STEMCELL Technologies) and cocultured with BMDCs for 4 to 5 days at 37 °C in RPMI media supplemented with 10% FBS, 100 U / mL penicillin, 100 μg / ml streptomycin, 50 μM β-mercaptoethanol, 1x MEM non-essential amino acids solution, 1% sodium pyruvate, 10 ng / mL TGF-b, and 100 IU / mL IL-2. For analysis of regulatory T cells, CD4+ T cells were harvested, washed with FACS buffer (1% BSA in PBS), stained for viability with LIVE / DEAD™ Fixable Dead Cell Stain (Invitrogen), incubated with anti-CD16 / 32, and stained with fluorophore-labelled antibodies against CD4 and CD25, followed by fixation and permeabilization for intracellular staining with fluorophore-labelled antibody against Foxp3. Cells were resuspended in FACS buffer and analysed by flow cytometry (ZE5). Adoptive Cell Transfer study: Spleens were harvested from transgenic OT-IIxThy1.1 mice. A single-cell suspension of splenocytes was prepared by disrupting the spleen with a syringe plunger through a 70um cell strainer. Red blood cells were lysed using ACK lysis buffer, and CD4+ T cells were isolated using EasySep™ Mouse CD4+ T Cell Isolation Kit (STEMCELL Technologies). Isolated CD4+ T cells were resuspended in ice cold PBS and injected retro- orbitally into naïve C57BL / 6 mice.1 day after the adoptive cell transfer, peptide, drug, or nanoparticles were subcutaneously administered.5 days later, blood was collected from the submandibular vein for PBMC analysis. Red blood cells were lysed using ACK lysis buffer, and remaining cells were washed with FACS buffer (1% BSA in PBS), stained for viability with LIVE / DEAD™ Fixable Dead Cell Stain (Invitrogen), incubated with anti-CD16 / 32, and stained with fluorophore-labelled antibodies against CD4, CD25, TCRVa2, and Thy1.1 (CD90.1), followed by fixation and permeabilization for intracellular staining with fluorophore-labelled antibody against Foxp3. Cells were resuspended in FACS buffer and analysed by flow cytometry (Cytek Aurora). EQUIVALENTS The invention may be embodied in other specific forms without departing from the spirit or essential characteristics thereof. The foregoing embodiments are therefore to be considered in all respects illustrative rather than limiting the invention described herein. Scope of the invention is thus indicated by the appended claims rather than by the foregoing description, and all changes that come within the meaning and range of equivalency of the claims are intended to be embraced therein. UM-43148.601 INCORPORATION BY REFERENCE The entire disclosure of each of the patent documents and scientific articles referred to herein is incorporated by reference for all purposes. The following references are herein incorporated by reference in their entireties:

Claims

UM-43148.601 CLAIMS 1. A composition comprising an sHDL nanoparticle associated with celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises a mixture of at least one phospholipid and at least one HDL apolipoprotein or apolipoprotein mimetic.

2. The composition of claim 1, wherein the phospholipid is selected from the group consisting of 1,2-dilauroyl-sn-glycero-3-phosphocholine; 1,2-dimyristoyl-sn-glycero-3- phosphocholine; 1,2-dipalmitoyl-sn-glycero-3-phosphocholine; 1,2-distearoyl-sn-glycero-3- phosphocholine; 1,2-diarachidoyl-sn-glycero-3-phosphocholine; 1,2-dibehenoyl-sn-glycero-3- phosphocholine; 1,2-dilignoceroyl-sn-glycero-3-phosphocholine; 1,2-dimyristoleoyl-sn-glycero- 3-phosphocholine; 1,2-dimyristelaidoyl-sn-glycero-3-phosphocholine; 1,2-dipalmitoleoyl-sn- glycero-3-phosphocholine; 1,2-dipalmitelaidoyl-sn-glycero-3-phosphocholine; 1,2- dipetroselenoyl-sn-glycero-3-phosphocholine; 1,2-dioleoyl-sn-glycero-3-phosphocholine; 1,2- dielaidoyl-sn-glycero-3-phosphocholine; 1,2-dieicosenoyl-sn-glycero-3-phosphocholine; 1,2- dinervonoyl-sn-glycero-3-phosphocholine; 1,2-dilauroyl-sn-glycero-3-phosphoethanolamine; 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine; 1,2-dipentadecanoyl-sn-glycero-3- phosphoethanolamine; 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine; 1,2-distearoyl-sn- glycero-3-phosphoethanolamine; 1,2-dipalmitoleoyl-sn-glycero-3-phosphoethanolamine; 1,2- dielaidoyl-sn-glycero-3-phosphoethanolamine; 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine; dioleoyl-sn-glycero-3-phosphoethanolamine-N-[3-(2-pyridyldithio) propionate]; 1,2- dipalmitoyl-sn-glycero-3-phosphothioethanol; 1,2-di-(9Z-octadecenoyl)-sn-glycero-3- phosphoethanolamine-N-[4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn-glycero- 3-phosphoethanolamine-N-[4-(p-maleimidophenyl)butyramide]; 1,2-dihexadecanoyl-sn- glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]; 1,2-di- (9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane- carboxamide]; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-[(3-Maleimide-1-oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Distearoyl; N-[(3-Maleimide-1- oxopropyl)aminopropyl polyethyleneglycol-carbamyl] distearoylphosphatidyl-ethanolamine; N- (3-Maleimide-1-oxopropyl)-L-α-phosphatidylethanolamine, Dimyristoy; N-(3-Maleimide-1- oxopropyl)-L-α-phosphatidylethanolamine, Dioleoyl; N-(3-Maleimide-1-oxopropyl)-L-α-UM-43148.601 phosphatidylethanolamine, Dipalmitoyl; N-(3-Maleimide-1-oxopropyl)-L-α- phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; phosphatidylcholine; phosphatidylinositol; phosphatidylserine; phosphatidylethanolamine; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Distearoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dioleoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, 1-Palmitoyl-2-oleoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dipalmitoyl; N-(Succinimidyloxy-glutaryl)-L-α- phosphatidylethanolamine, Dimyristoyl; 3-(N-succinimidyloxyglutaryl)aminopropyl, and polyethyleneglycol-carbamyl distearoylphosphatidyl-ethanolamine; N-(3-oxopropoxy polyethyleneglycol)carbamyl-distearoyl-ethanolamine.

3. The composition of claim 1, wherein the HDL apolipoprotein component is selected from the group consisting of apolipoprotein A-I (apoA-I), apolipoprotein A-II (apoA-II), apolipoprotein A-II xxx (apoA-II-xxx), apolipoprotein A4 (apoA4), apolipoprotein Cs (apoCs), apolipoprotein E (apoE), apolipoprotein A-I milano (apoA-I-milano), apolipoprotein A-I paris (apoA-I-paris), apolipoprotein M (apoM), an HDL apolipoprotein mimetic, preproapoliprotein, preproApoA-I, proApoA I, preproApoA-II, proApoA II, preproApoA-IV, proApoA-IV, ApoA- V, preproApoE, proApoE, preproApoA IMilano, proApoA-IMilano, preproApoA-IParis, proApoA- IParis, and mixtures thereof.

4. The composition of claim 1, wherein the apolipoprotein mimetic is described by any of SEQ ID NOs: 1-336 and WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341), LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358),UM-43148.601 LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373).

5. The composition of claim 1, further comprising a plurality of peptide antigens associated with (e.g., complexed, conjugated, encapsulated, absorbed, adsorbed, admixed) the sHDL nanoparticle.

6. The composition of claim 5, wherein the plurality of peptide antigen is a plurality of tolerogenic antigens.

7. The composition of claim 6, wherein the plurality of tolerogenic antigens are tolerogenic antigens comprising between 3 amino acids and 50 amino acids in length.

8. The composition of claim 6, wherein the plurality of tolerogenic antigens are tolerogenic antigens comprising a polypeptide comprising a nucleic acid sequence of any one of SEQ ID NOs: 375-796.

9. The composition of claim 6, wherein the plurality of tolerogenic antigens are human allograft transplantation antigens.

10. The composition of claim 9, wherein the human allograft transplantation antigens are selected from subunits of the various MHC class I and MHC class II haplotype proteins, andUM-43148.601 single-amino-acid polymorphisms on minor blood group antigens including RhCE, Kell, Kidd, Duffy and Ss.

11. The composition of claim 6, wherein the plurality of tolerogenic antigens are specific for type 1 diabetes mellitus.

12. The composition of claim 11, wherein the plurality of tolerogenic antigens are selected from insulin, proinsulin, pre-proinsulin, glutamic acid decarboxylase-65 (GAD-65), GAD-67, insulinoma-associated protein 2 (IA-2), insulinoma-associated protein 213 (IA-213), ICA69, ICA12 (SOX-13), carboxypeptidase H, Imogen 38, GLIMA 38, chromogranin-A, HSP-60, caboxypeptidase E, peripherin, glucose transporter 2, hepatocarcinoma-intestine- pancreas / pancreatic associated protein, S10013, glial fibrillary acidic protein, regenerating gene II, pancreatic duodenal homeobox 1, dystrophia myotonica kinase, islet-specific glucose-6- phosphatase catalytic subunit-related protein, and SST G-protein coupled receptors 1-5.

13. The composition of claim 6, wherein the plurality of tolerogenic antigens are specific for one or more of the following autoimmune disorders: rheumatoid arthritis, multiple sclerosis, diabetes, autoimmune diseases of the thyroid, thyroid-associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutieres syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease.

14. The composition of claim 6, wherein the plurality of tolerogenic antigens comprises one or more of tolerogenic antigens selected from thyroglobulin (TG), thyroid peroxidase (TPO), thyrotropin receptor (TSHR), sodium iodine symporter (NIS), megalin, thyroid autoantigens including TSHR, insulin-like growth factor 1 receptor, calcium sensitive receptor, 21- hydroxylase, 17a-hydroxylase, and P450 side chain cleavage enzyme (P450scc), ACTHUM-43148.601 receptor, P450c21, P450c17, FSH receptor, a-enolase, pituitary gland-specific protein factor (PGSF) 1 a and 2, and type 2 iodothyronine deiodinase, myelin basic protein, myelin oligodendrocyte glycoprotein, proteolipid protein, collagen II, W, K+-ATPase, tissue transglutaminase and gliadin, tyrosinase, tyrosinase related protein 1 and 2, acetylcholine receptor, desmoglein 3, 1 and 4, pemphaxin, desmocollins, plakoglobin, perplakin, desmoplakins, acetylcholine receptor, BP180, BP230, plectin, laminin 5, endomysium, tissue transglutaminase, collagen VII, matrix metalloproteinase 1 and 3, the collagen-specific molecular chaperone heat-shock protein 47, fibrillin-1, PDGF receptor, Scl-70, U1 RNP, Th / To, Ku, Jo 1, NAG-2, centromere proteins, topoisomerase I, nucleolar proteins, RNA polymerase I, II and Ill, PM-Sic, fibrillarin, 823, U1snRNP, nuclear antigens SS-A and SS-8, fodrin, poly(ADP-ribose) polymerase, topoisomerase, nuclear proteins including SS-A, high mobility group box 1 (HMGB1), nucleosomes, histone proteins, double-stranded DNA, glomerular basement membrane proteins including collagen IV, cardiac myosin, aromatic L-amino acid decarboxylase, histidine decarboxylase, cysteine sulfinic acid decarboxylase, tryptophan hydroxylase, tyrosine hydroxylase, phenylalanine hydroxylase, hepatic P450 cytochromes P4501A2 and 2A6, SOX-9, SOX-10, calcium-sensing receptor protein, and type 1 interferons interferon alpha, beta and omega.

15. The composition of claim 6, wherein the plurality of tolerogenic antigens are specific for celiac disease.

16. The composition of claim 6, wherein the plurality of tolerogenic antigens are selected from gliadin, glutenin, and fragments thereof capable of inducing an immune response.

17. The method of Claim 6, wherein the plurality of tolerogenic antigens are conjugated to the outer surface of the sHDL nanoparticle.

18. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid.

19. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid via a linker.

20. The composition of claim 19, wherein the linker is selected from non-ester containingUM-43148.601 linker moieties and ester-containing linker moieties.

21. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is non-covalently attached to the phospholipid.

22. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is admixed with the sHDL.

23. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is adsorbed onto or into the sHDL.

24. The composition of claim 1, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is encapsulated within the sHDL.

25. The method of Claim 1, wherein the average particle size of the sHDL nanoparticle is between 6 to 500 nm.

26. A composition comprising an sHDL nanoparticle comprising celastrol (or a variant thereof) and / or rapamycin (or a variant thereof), wherein the sHDL nanoparticle comprises at least one phospholipid selected from 1,2- dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC), and at least one HDL apolipoprotein or apolipoprotein mimetic.

27. The composition of claim 26, wherein the HDL apolipoprotein component is selected from the group consisting of apolipoprotein A-I (apoA-I), apolipoprotein A-II (apoA-II), apolipoprotein A-II xxx (apoA-II-xxx), apolipoprotein A4 (apoA4), apolipoprotein Cs (apoCs), apolipoprotein E (apoE), apolipoprotein A-I milano (apoA-I-milano), apolipoprotein A-I paris (apoA-I-paris), apolipoprotein M (apoM), an HDL apolipoprotein mimetic, preproapoliprotein, preproApoA-I, proApoA I, preproApoA-II, proApoA II, preproApoA-IV, proApoA-IV, ApoA- V, preproApoE, proApoE, preproApoA IMilano, proApoA-IMilano, preproApoA-IParis, proApoA- IParis, and mixtures thereof.

28. The composition of claim 26, wherein the apolipoprotein mimetic is described by any of SEQ ID NOs: 1-336 and WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341),UM-43148.601 LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358), LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373). 29 The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid.

30. The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid via a linker.

31. The composition of claim 30, wherein the linker is selected from non-ester containing linker moieties and ester-containing linker moieties.UM-43148.601 32. The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is non-covalently attached to the phospholipid.

33. The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is admixed with the sHDL.

34. The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is adsorbed onto or into the sHDL.

35. The composition of claim 26, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is encapsulated within the sHDL.

36. The method of Claim 26, wherein the average particle size of the sHDL nanoparticle is between 6 to 500 nm.

37. A composition comprising an sHDL nanoparticle comprising celastrol (or variant thereof) and / or rapamycin (or a variant thereof), at least one phospholipid selected from 1,2-dimyristol-sn-glycero-3-phosphocholine (DPMC) and dipalmitoylphosphatidylcholine (DPPC), and at least one HDL apolipoprotein or apolipoprotein mimetic, and a plurality of tolerogenic antigens.

38. The composition of claim 37, wherein the HDL apolipoprotein component is selected from the group consisting of apolipoprotein A-I (apoA-I), apolipoprotein A-II (apoA-II), apolipoprotein A-II xxx (apoA-II-xxx), apolipoprotein A4 (apoA4), apolipoprotein Cs (apoCs), apolipoprotein E (apoE), apolipoprotein A-I milano (apoA-I-milano), apolipoprotein A-I paris (apoA-I-paris), apolipoprotein M (apoM), an HDL apolipoprotein mimetic, preproapoliprotein, preproApoA-I, proApoA I, preproApoA-II, proApoA II, preproApoA-IV, proApoA-IV, ApoA- V, preproApoE, proApoE, preproApoA IMilano, proApoA-IMilano, preproApoA-IParis, proApoA- IParis, and mixtures thereof.

39. The composition of claim 37, wherein the apolipoprotein mimetic is described by any of SEQ ID NOs: 1-336 and WDRVKDLATVYVDVLKDSGRDYVSQF (SEQ ID NO:341),UM-43148.601 LKLLDNWDSVTSTFSKLREOL (SEQ ID NO:342), PVTOEFWDNLEKETEGLROEMS (SEQ ID NO:343), KDLEEVKAKVQ (SEQ ID NO: 344), KDLEEVKAKVO (SEQ ID NO: 345), PYLDDFQKKWQEEMELYRQKVE (SEQ ID NO: 346), PLRAELQEGARQKLHELOEKLS (SEQ ID NO: 347), PLGEEMRDRARAHVDALRTHLA (SEQ ID NO: 348), PYSDELRQRLAARLEALKENGG (SEQ ID NO: 349), ARLAEYHAKATEHLSTLSEKAK (SEQ ID NO: 350), PALEDLROGLL (SEQ ID NO: 351), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), PVLESFVSFLSALEEYTKKLN (SEQ ID NO:353), PVLESFKVSFLSALEEYTKKLN (SEQ ID NO:352), TVLLLTICSLEGALVRRQAKEPCV (SEQ ID NO: 354) QTVTDYGKDLME (SEQ ID NO:355), KVKSPELOAEAKSYFEKSKE (SEQ ID NO:356), VLTLALVAVAGARAEVSADOVATV (SEQ ID NO:357), NNAKEAVEHLOKSELTOOLNAL (SEQ ID NO:358), LPVLVWLSIVLEGPAPAOGTPDVSS (SEQ ID NO:359), LPVLVVVLSIVLEGPAPAQGTPDVSS (SEQ ID NO:360), ALDKLKEFGNTLEDKARELIS (SEQ ID NO: 361), VVALLALLASARASEAEDASLL (SEQ ID NO:362), HLRKLRKRLLRDADDLQKRLAVYOA (SEQ ID NO:363), AQAWGERLRARMEEMGSRTRDR (SEQ ID NO:364), LDEVKEQVAEVRAKLEEQAQ (SEQ ID NO:365), DWLKAFYDKVAEKLKEAF (SEQ ID NO:236), DWLKAFYDKVAEKLKEAFPDWAKAAYDKAAEKAKEAA (SEQ ID NO:366), PVLDLFRELLNELLEALKQKL (SEQ ID NO:367), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:368), PVLDLFRELLNELLEALKQKLK (SEQ ID NO:4), PVLDLFRELLNELLEALKQKLA (SEQ ID NO:369), PVLDLFRELLNELLEALKKLLK (SEQ ID NO:370), PVLDLFRELLNELLEALKKLLA (SEQ ID NO:371), PLLDLFRELLNELLEALKKLLA (SEQ ID NO:372), and EVRSKLEEWFAAFREFAEEFLARLKS (SEQ ID NO: 373).

40. The composition of claim 37, wherein the plurality of tolerogenic antigens are tolerogenic antigens comprising between 3 amino acids and 50 amino acids in length.

41. The composition of claim 37, wherein the plurality of tolerogenic antigens are tolerogenic antigens comprising a polypeptide comprising a nucleic acid sequence of any one of SEQ ID NOs: 375-796.UM-43148.601 42. The composition of claim 37, wherein the plurality of tolerogenic antigens are human allograft transplantation antigens.

43. The composition of claim 42, wherein the human allograft transplantation antigens are selected from subunits of the various MHC class I and MHC class II haplotype proteins, and single-amino-acid polymorphisms on minor blood group antigens including RhCE, Kell, Kidd, Duffy and Ss.

44. The composition of claim 37, wherein the plurality of tolerogenic antigens are specific for type 1 diabetes mellitus.

45. The composition of claim 44, wherein the plurality of tolerogenic antigens are selected from insulin, proinsulin, pre-proinsulin, glutamic acid decarboxylase-65 (GAD-65), GAD-67, insulinoma-associated protein 2 (IA-2), insulinoma-associated protein 213 (IA-213), ICA69, ICA12 (SOX-13), carboxypeptidase H, Imogen 38, GLIMA 38, chromogranin-A, HSP-60, caboxypeptidase E, peripherin, glucose transporter 2, hepatocarcinoma-intestine- pancreas / pancreatic associated protein, S10013, glial fibrillary acidic protein, regenerating gene II, pancreatic duodenal homeobox 1, dystrophia myotonica kinase, islet-specific glucose-6- phosphatase catalytic subunit-related protein, and SST G-protein coupled receptors 1-5.

46. The composition of claim 37, wherein the plurality of tolerogenic antigens are specific for one or more of the following autoimmune disorders: rheumatoid arthritis, multiple sclerosis, diabetes, autoimmune diseases of the thyroid, thyroid-associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutieres syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease.UM-43148.601 47. The composition of claim 37, wherein the plurality of tolerogenic antigens comprises one or more of tolerogenic antigens selected from thyroglobulin (TG), thyroid peroxidase (TPO), thyrotropin receptor (TSHR), sodium iodine symporter (NIS), megalin, thyroid autoantigens including TSHR, insulin-like growth factor 1 receptor, calcium sensitive receptor, 21- hydroxylase, 17a-hydroxylase, and P450 side chain cleavage enzyme (P450scc), ACTH receptor, P450c21, P450c17, FSH receptor, a-enolase, pituitary gland-specific protein factor (PGSF) 1 a and 2, and type 2 iodothyronine deiodinase, myelin basic protein, myelin oligodendrocyte glycoprotein, proteolipid protein, collagen II, W, K+-ATPase, tissue transglutaminase and gliadin, tyrosinase, tyrosinase related protein 1 and 2, acetylcholine receptor, desmoglein 3, 1 and 4, pemphaxin, desmocollins, plakoglobin, perplakin, desmoplakins, acetylcholine receptor, BP180, BP230, plectin, laminin 5, endomysium, tissue transglutaminase, collagen VII, matrix metalloproteinase 1 and 3, the collagen-specific molecular chaperone heat-shock protein 47, fibrillin-1, PDGF receptor, Scl-70, U1 RNP, Th / To, Ku, Jo 1, NAG-2, centromere proteins, topoisomerase I, nucleolar proteins, RNA polymerase I, II and Ill, PM-Sic, fibrillarin, 823, U1snRNP, nuclear antigens SS-A and SS-8, fodrin, poly(ADP-ribose) polymerase, topoisomerase, nuclear proteins including SS-A, high mobility group box 1 (HMGB1), nucleosomes, histone proteins, double-stranded DNA, glomerular basement membrane proteins including collagen IV, cardiac myosin, aromatic L-amino acid decarboxylase, histidine decarboxylase, cysteine sulfinic acid decarboxylase, tryptophan hydroxylase, tyrosine hydroxylase, phenylalanine hydroxylase, hepatic P450 cytochromes P4501A2 and 2A6, SOX-9, SOX-10, calcium-sensing receptor protein, and type 1 interferons interferon alpha, beta and omega.

48. The composition of claim 37, wherein the plurality of tolerogenic antigens are specific for celiac disease.

49. The composition of claim 37, wherein the plurality of tolerogenic antigens are selected from gliadin, glutenin, and fragments thereof capable of inducing an immune response.

50. The method of Claim 37, wherein the plurality of tolerogenic antigens are conjugated to the outer surface of the sHDL nanoparticle.

51. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid.UM-43148.601 52. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is covalently attached to the phospholipid via a linker.

53. The composition of claim 52, wherein the linker is selected from non-ester containing linker moieties and ester-containing linker moieties.

54. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is non-covalently attached to the phospholipid.

55. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is admixed with the sHDL.

56. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is adsorbed onto or into the sHDL.

57. The composition of claim 37, wherein the celastrol (or a variant thereof) and / or rapamycin (or a variant thereof) is encapsulated within the sHDL.

58. The method of Claim 37, wherein the average particle size of the sHDL nanoparticle is between 6 to 500 nm.

59. A method for treating and / or preventing a condition, disorder, and / or disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

60. The method of claim 59, wherein the condition, disorder, and / or disease is selected from erythropoietic porphyries, T2 diabetes, antifibrinolytic, central diabetes insipidus, delaying the birth in case of threat of premature birth, antibiotic, cystic fibrosis, angina, anticoagulant in patients with unstable angina undergoing PTCA or PCI, systemic lupus erythematosus, hypercalcemia, osteoporosis, pagets disease, carbetocin works as an oxytocic, antihemorrhagic and uterotonic drug in the peripheral nervous system, prevention of uterine atony, induction, and control postpartum bleeding or haemorrhage, stimulant of the gastric secretion, for treat hormone-sensitive cancers of the prostate and breast, inhibition of premature LH surges inUM-43148.601 women undergoing controlled ovarian stimulation, immunosuppression in organ transplantation to prevent rejection, peritumoral brain edema, diagnosis of ACTHdependent Cushing’s syndrome, allergies, ankylosing spondylitis, psoriasis, chorioditis, erythema, keratitis, sclerosis, dermatomyositis, rheumatoid arthritis, Stevens-Johnson Syndrome, ulcerative colitis, diagnosis of adrenocortical insufficiency, antibiotic, systemic infections caused by gram positive organisms, nocturnal enuresis, nocturia, and stoppage of bleeding or haemorrhage in haemophilia A patients, acute hereditary angioderma, postmenopausal osteoporosis, anti- parathyroid, Paget’s disease, hypercalcaemia, hypertension, AIDS / HIV-1 infection, acute coronary syndrome, unstable angina undergoing PCI, Alzheimer’s and Parkinson’s disease, inhibition of premature LH surges in women undergoing controlled ovarian hyperstimulation, Relapsing- Remitting Multiple Sclerosis, hepatic insufficiency, wound healing, inflammation of respiratory tract, asthenia, release of follicle-stimulating hormone (FSH) and luteinizing hormone (LH) from the anterior pituitary, stimulate the secretion of gonadotropin during disturbances fertility, and diagnosis of the functional capacity and response of the gonadotropes of the anterior pituitary, for skin lesions, surface wounds and eye infections, postmenopausal osteoporosis, Paget’s disease, hypercalcaemia, hereditary angioedema, immune system related diseases, acromegaly, anticoagulant, fibroids and endometriosis, central diabetes insipidus, Cushing’s syndrome, diabetic foot ulcers, treatment of central precocious puberty, uterine fibriods and endometriosis, vasodilatory, natriuretic, diuretic and neurohormonal effects, acromegaly, carcinoid syndrome, acute bacterial skin and skin structure infections, initiation or improvement of uterine contractions, and control postpartum bleeding or haemorrhage, hematide Chronic kidney disease associated anemia, stomatitis, pharyngitis, diagnostic assessment of thyroid function, postmenopausal osteoporosis, hypercalcaemia, diagnosis of pancreatic exocrine dysfunction, and gastrinoma, Zollinger-Ellison syndrome, prevention of RDS in premature infants, and meconium aspiration syndrome, acute variceal bleeding, allergic rhinitis and conjunctivitis, spinocerebellar degeneration / ataxia, Short Bowel Syndrome, antibiotic, bactericidal, teriparatide is the only anabolic (i.e., bone growing) agent indicated for use in postmenopausal women with osteoporosis, Cortrosyn Analogue of adrenocorticotrophic hormone (ACTH) used for diagnostic purposes, treatment of adrenal insufficiency, epilepsia, Chronic hepatitis B, chronic hepatitis C, primary and secondary immune deficiencies, acute decompensated heart failure, colitis, esophageal variceal bleeding in patients with cirrhotic liver disease and AIDS-related diarrhea, sarcoidosis and acute lung injury, and severe chronic pain.

61. A method for treating and / or preventing arthritis and / or rheumatoid arthritis in a subjectUM-43148.601 (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

62. A method for treating and / or preventing eczema in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

63. A method for treating and / or preventing tuberculosis in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

64. A method for treating and / or preventing obesity in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

65. A method for treating and / or preventing Crohn’s disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

66. A method for treating and / or preventing prostate cancer in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

67. A method for treating and / or preventing organ transplant rejection in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

68. A method for treating and / or preventing an autoimmune disorder in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

69. The method of claim 68, wherein the autoimmune disorder is selected from multiple sclerosis (MS), celiac disease, rheumatoid arthritis, diabetes (e.g., type 1 diabetes mellitus), autoimmune diseases of the thyroid (e.g., Hashimoto's thyroiditis, Graves' disease), thyroid-UM-43148.601 associated ophthalmopathy and dermopathy, hypoparathyroidism, Addison's disease, premature ovarian failure, autoimmune hypophysitis, pituitary autoimmune disease, immunogastritis, pernicious angemis, celiac disease, vitiligo, myasthenia gravis, pemphigus vulgaris and variants, bullous pemphigoid, dermatitis herpetiformis Duhring, epidermolysis bullosa acquisita, systemic sclerosis, mixed connective tissue disease, Sjogren's syndrome, systemic lupus erythematosus, Goodpasture's syndrome, rheumatic heart disease, autoimmune polyglandular syndrome type 1, Aicardi-Goutières syndrome, Acute pancreatitis Age-dependent macular degeneration, Alcoholic liver disease, Liver fibrosis, Metastasis, Myocardial infarction, Nonalcoholic steatohepatitis (NASH), Parkinson's disease, Polyarthritis / fetal and neonatal anemia, Sepsis, and inflammatory bowel disease.

70. A method for treating and / or preventing an inflammatory disorder in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

71. The method of claim 70, wherein the inflammatory disorder is selected from idiopathic inflammatory diseases or disorders, chronic inflammatory diseases or disorders, acute inflammatory diseases or disorders, autoimmune diseases or disorders, infectious diseases or disorders, inflammatory malignant diseases or disorders, inflammatory transplantation-related diseases or disorders, inflammatory degenerative diseases or disorders, diseases or disorders associated with a hypersensitivity, inflammatory cardiovascular diseases or disorders (e.g., as described herein), inflammatory cerebrovascular diseases or disorders, peripheral vascular diseases or disorders, inflammatory glandular diseases or disorders, inflammatory gastrointestinal diseases or disorders, inflammatory cutaneous diseases or disorders, inflammatory hepatic diseases or disorders, inflammatory neurological diseases or disorders, inflammatory musculo-skeletal diseases or disorders, inflammatory renal diseases or disorders, inflammatory reproductive diseases or disorders, inflammatory systemic diseases or disorders, inflammatory connective tissue diseases or disorders, inflammatory tumors, necrosis, inflammatory implant-related diseases or disorders, inflammatory aging processes, immunodeficiency diseases or disorders, proliferative diseases and disorders, and inflammatory pulmonary diseases or disorders.UM-43148.601 72. A method for treating and / or preventing diabetes in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

73. A method for treating and / or preventing celiac disease in a subject (e.g., a human subject), comprising administering to the subject a therapeutically effective amount of a composition recited in claim 1, claim 26, or claim 37.

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