445 results about "Inhibitory peptide" patented technology

The present invention provides peptide analogs and peptide mimetics that inhibit pleated sheet formation in amyloid beta-peptide, pharmaceutical compositions thereof and their therapeutic use. The inhibitory peptides possess activity as inhibitors in the formation of amyloid-like deposits and are useful in the treatment of Alzheimer's Disease.

Disclosed are peptides that inhibit the enzymatic activity of tyrosinase, as well as formulations and methods for their use in the reduction of skin pigmentation, and methods of administering the inhibitory peptides in a topical formulation. Peptide sequences disclosed include KFEKKFEK and YRSRKYSSWY.

A method for preparing ACE inhibition peptides from fish skin is provided. The method is prepared with tilapia skin, extracts fish skin albumen from tilapia skin, adapts prolease to hydrolysis through enzyme extinguishing, debitterizing, decolouring, de-flavoring, filtering, ion exchanging and concentrating to obtain fish skin proteolysis liquor, after untruly filter (cutoff molecular mass is 9000Da) the TSP-I, collect high activity component by SephadexG-15 gel chromatography, freeze and dry to obtain high activity ACE inhibition peptides. The invention has important meaning for satisfying integrated utilization of tilapia skin wastes and improving its attachment.

The invention provides peptides that bind Tissue Factor Pathway Inhibitor (TFPI), including TFPI-inhibitory peptides, and compositions thereof. The peptides may be used to inhibit a TFPI, enhance thrombin formation in a clotting factor-deficient subject, increase blood clot formation in a subject, and / or treat a blood coagulation disorder in a subject.

The invention provides methods for designing peptides that inhibit aggregation in target polypeptides. The candidate inhibitory peptidic compounds have an oligomeric sequence that forms energetically-favorable interactions with the amino acid sequence of the steric zipper region of the target protein, and also possess a zipper-disrupting feature that disrupt the peptide stacking at the steric zipper region. This method can be used to obtain inhibitory peptides to disrupt fibril formation involving any protein for which a steric zipper sequence can be identified. The invention also provides inhibitory peptidic compounds, which can be used in pharmaceutical compositions and methods for treating polypeptide aggregation-associated diseases or conditions.

The present invention provides a method for the screening of nucleic acid fragment expression libraries and selecting encoded peptides based upon their ability to modulate the activity of a target protein or nucleic acid and assume conserved conformations compatible with albeit not reiterative of the target protein or nucleic acid. The present invention also provides methods for the diagnosis and treatment of ischemia. The present invention also provides c-Jun dimerization inhibitory peptides and analogues thereof that are useful for treatment of ischemia.

The invention discloses an angiotensin converting enzyme inhibitory peptide, which is characterized by comprising the following amino acid sequences: SEQ NO1: Arg-Leu-Ser-Phe-Asn-Pro, SEQ NO2: Leu-Leu, and SEQ NO3: Ala-Leu-Pro-Met-His-Ile-Arg. The method for preparing the inhibitory peptides comprises the following steps of: (1) preparing lactalbumin concentrated solution; (2) preparing lactalbumin hydrolysis liquid; (3) preparing angiotensin converting enzyme-containing inhibitory peptide concentrated solution; (4) performing separation and purification on the inhibitory peptide-containing concentrated solution through gel chromatography and reverse-phase high-pressure liquid chromatography; and (5) obtaining the product by freeze drying. The invention has the advantages that: three amino acid sequences of the angiotensin converting enzyme inhibitory peptide derived from the lactalbumin are disclosed for the first time, the preparation cost is low and the extraction ratio is high.

There is provided a series of novel substituted gamma-lactams of Formula (I) wherein R1, R2, R3, R4 and R5 are defined herein, their pharmaceutical compositions and methods of use. These novel compounds inhibit the processing of amyloid precursor protein (APP) by β-secretase and, more specifically, inhibit the production of Aβ-peptide. The present invention is directed to compounds useful in the treatment of neurological disorders related to β-amyloid production, such as Alzheimer's disease and other conditions affected by anti-amyloid activity.

The invention discloses a novel orally-effective spirulina source antihypertensive peptide and a preparation method thereof. The antihypertensive peptide is a tripeptide with the sequence of isoleucine-glutamine-proline (Ile-Gln-Pro, IQP). An angiotensin converting enzyme (ACE) inhibitory peptide is prepared by the following steps of: performing enzymolysis on spirulina platensis by adopting alkali protease, and performing ultrafiltration, gel filtration chromatography and secondary reversed phase high-performance liquid chromatography purification. Tests prove that the IQP is a noncompetitive inhibitor of ACE, and can keep good ACE inhibitory activity under digestion of main gastrointestinal protease. The IQP has good antihypertensive effect on essential hypertension rat (SHR) and has great application prospects in medicaments and functional foods for preventing and treating hypertension.

The invention discloses a method for preparing a DPP-IV inhibitory peptide through using hairtail. The method is characterized in that the method comprises the following steps: adding water to hairtail, and rubbing to form a uniform fish flesh pulp; putting the fish flesh pulp in an enzymatic hydrolysis tank, adding endo protease, and carrying out stirring hydrolysis for 4-12h to obtain a hydrolysate; heating to 95-100DEG C, and maintaining the temperature unchanged for 10-15min for enzyme killing; cooling the hydrolysate to 40-60DEG C, adding exoproteinase, and carrying out stirring hydrolysis for 2-8h; heating to 95-100DEG C, and maintaining the temperature unchanged for 10-15min for enzyme killing; centrifuging the obtained enzyme-killed hydrolysate, and taking the obtained supernatant; adding the supernatant to an ultrafilter membrane separator, adjusting the pressure and the interception molecular weight of the ultrafilter membrane to 0.05-0.1MPa and 3000Da respectively, and collecting an ultrafilter membrane permeate liquid; and separating and purifying the DPP-IV inhibitory peptide through adopting an affinity chromatography process. The method has the advantages of simple technology, low production cost and short production period.

Intravitreal administration of a JNK-inhibitory peptide less than 150 amino acids in length, containing at least one D-amino acid, and having (a) a JNK-inhibitory sequence of at least any of SEQ ID NO: 1 and SEQ ID NO: 2, and (b) a transport sequence of at least any of SEQ ID NO: 3 and SEQ ID NO: 4 suppressed spermidine-induced retinal pigment epithelial damage, tunicamycin-induced photoreceptor cell damage, and laser-induced choroidal neovascularization. Thus, the JNK-inhibitory peptide of the present invention is useful for prophylaxis or therapy of a retinal disease. By the use of this JNK-inhibitory peptide, a drug and a method are provided which are capable of preventing or treating a retinal disease even by topical administration to the eye, and use of the JKN-inhibitory peptide for manufacturing the drug is also provided.

The present invention provides compositions comprising peptidyl inhibitors of CD40L-dependent signalling that are not derived from a natural binding partner of CD40L such as CD40, or from a native CD40-CD40L interface. More particularly, the peptidyl inhibitors of the present invention are derived from natural sources that do not express CD40-CD40L costimulatory pathways. The invention also provides synthetic derivatives and analogs of the peptidyl inhibitors having enhanced binding affinity for CD40L or enhanced inhibitory activity relative to their parent molecules.

The present invention relates to compounds of the Formula I wherein R1, R3, R5, R7, X, Y and U are as defined. Compounds of the Formula I have activity inhibiting production of Aβ-peptide. The invention also relates to pharmaceutical compositions and methods of treating diseases and disorders, for example, neurodegenerative and / or neurological disorders, e.g., Alzheimer's disease, in a mammal comprising compounds of the Formula I.

The invention relates to a tumor inhibitory peptide capable of being specifically bound with PD-1 and an application thereof. The inhibitory peptide can be bound with an extracellular region of a PD-1 protein receptor and can effectively close a PD-1 protein at protein level and cellular level and prevent the PD-1 protein from being bound with a ligand PD-L1. The polypeptide has good biological activity. The polypeptide can be used in tumor immunotherapy alone or combined with an anti-PD-1 monoclonal antibody or other anti-tumor drugs as well as diagnosis and screening of a PD-1 positive tumor patient, namely the polypeptide can be applied to preparation of drugs used for treating tumor and autoimmune diseases.

The present invention provides peptide analogues which are antagonists of gastric inhibitory peptide (GIP). The peptides, based on GIP 1-42 include substitutions and / or modifications which have enhanced resistance to degradation by the enzyme dipeptidyl peptidase IV (DPP IV). The invention also provides a process of N terminally modifying GIP and the use of the peptide analogues for treatment of diabetes.

The invention provides polypeptides (e.g., antibodies) and fusion proteins that target a epitope in the receptor binding domain (RBD) of the spike (S) glycoprotein of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV). The polypeptides and fusion proteins can be used to treat and prevent MERS-CoV infection in mammals.

Disclosed are methods for treating Alzheimer's disease, and other diseases, and / or inhibiting beta-secretase enzyme, and / or inhibiting deposition of A beta peptide in a mammal, by use of 3,4-disubstituted piperidinyl compounds of formula (I) wherein the variables R1, R2, R3, R4, Q, W, X, Z, m, and n are defined herein.

The invention aims at providing a novel angiotensin-converting enzyme inhibition peptide, namely an ACE inhibition peptide prepared form isochrysis galbana, and with the amino acid sequence of SEQ ID NO:1. The invention provides a preparation method of a high-activity angiotensin-converting enzyme inhibition peptide sourcing from marine microalgae. The current angiotensin-converting enzyme inhibiter mainly comes from food and large macroalgae of laver and the like, and coming from bait microalgae is not reported. The structure of the obtained active peptide with a unique structure is Tyr-Met-Gly-Leu-Asp-Leu-Lys. The structure is novel and has the characteristics of being small in molecular weight and easily absorbed by a human body.

The invention provides peptides that bind Tissue Factor Pathway Inhibitor (TFPI), including TFPI-inhibitory peptides, and compositions thereof. The peptides may be used to inhibit a TFPI, enhance thrombin formation in a clotting factor-deficient subject, increase blood clot formation in a subject, treat a blood coagulation disorder in a subject, purify TFPI, and identify a TFPI-binding compound.

Methods for treating arthritis comprising 14-3-3 antagonists that are capable of specifically binding to extracellularly localized 14-3-3 eta and / or 14-3-3 gamma protein isoforms are provided. In preferred embodiments, the 14-3-3 antagonist is an inhibitory peptide or an anti-14-3-3 antibody. The 14-3-3 antagonists are also formulated in a pharmaceutical composition and used in a method for reducing matrix metalloprotease (MMP) expression in the synovial fluid of a patient, wherein the MMP is MMP-1 or MMP-3.

The invention discloses an angiotensin-converting enzyme inhibitory peptide, and a preparation method and an application thereof, wherein the amino acid sequence of the inhibitory peptide is Leu-Ala-Ser-Pro-Thr-Met. The angiotensin-converting enzyme inhibitory peptide is prepared by tracking, screening and estimating an active ingredient for inhibiting the angiotensin-converting enzyme in mactra veneriformis by virtue of modern biochemical technical means, and purifying the active ingredient by methods of enzymolysis, ultrafiltration, reversed-phase high-performance liquid chromatography and the like; and experiment results indicate that the inhibitory peptide has an excellent effect of inhibiting the angiotensin-converting enzyme and a good anti-hypertension effect, and is good in safety performance, and thus has a bright application prospect.

The invention provides a method for preparing ACE (Angiotensin Converting Enzyme) inhibitory peptides through bean pulp enzymolysis. The method comprises the following steps that (1) high-temperature bean pulp is crushed and sieved, obtained bean pulp powder and water are mixed according to a mass ratio of 1:(4-6), the pH value is regulated to 8 to 10, and a bean pulp mixture is obtained; (2) the pH value of the bean pulp mixture is regulated to 7 to 9, a complex enzyme preparation is added, the mixture is uniformly mixed, hydrolysis is carried out for 5 to 8 hours at the temperature being 35 to 50 DEG C, after the hydrolysis is completed, hydrolysis liquid is boiled in a boiling water bath for enzyme deactivation, and mixed liquid is obtained; (3) the pH value of the mixed liquid is regulated to 6.5 to 7.5, supernatant is taken, ultrafiltration treatment is performed through an ultrafiltration membrane, and filtered liquid is obtained; and (4) the filtered liquid is subjected to vacuum freezing drying, and the ACE inhibitory peptide powder is obtained. The method for preparing ACE inhibitory peptides through bean pulp enzymolysis has the advantages that the process is simple and is easy to implement; in the whole process, the reaction conditions are mild; the compounded complex enzyme preparation is used; and the industrial processing operation is convenient.

This invention relates to novel lactams of Formula (I): having drug and bio-affecting properties, their pharmaceutical compositions and methods of use. These novel compounds inhibit the processing of amyloid precursor protein and, more specifically, inhibit the production of Aβ-peptide, thereby acting to prevent the formation of neurological deposits of amyloid protein. More particularly, the present invention relates to the treatment of neurological disorders related to β-amyloid production such as Alzheimer's disease and Down's Syndrome.

A method of treating chemotherapy-induced thrombocytopenia includes administering to a subject undergoing chemotherapy a therapeutically effective amount of a Bax-inhibiting peptide.

There is provided a series of novel macrocyclic diaminopropanes of Formula (I) or a stereoisomer; or a pharmaceutically acceptable salt thereof, wherein R1, R2, R4, R5, n, L, Z, and as defined herein, their pharmaceutical compositions and methods of use. These novel compounds inhibit the processing of amyloid precursor protein (APP) by β-secretase and, more specifically, inhibit the production of Aβ-peptide. The present disclosure is directed to compounds useful in the treatment of neurological disorders related to β-amyloid production, such as Alzheimer's disease and other conditions affected by anti-amyloid activity.