22 results about "Immunomodulatory peptide" patented technology

The invention provides an allosteric nanogel adjuvant as well as a preparation method and application thereof, and belongs to the technical field of vaccines. The allosteric nanogel adjuvant comprises a self-assembly motif, a responsive site and an immunomodulatory peptide fragment, and the self-assembly motif is composed of 2-5 amino acids; the allosteric nanogel adjuvant has a structure as shown in a formula I, and is named as NTP5 for short; the allosteric nanogel adjuvant is self-assembled into nanoparticles, the nanoparticles are allosteric into a nanofiber structure through responsive broken bonds, nanogel is further formed, and the key problems of a traditional vaccine in the aspects of antigen delivery and immune activation are effectively solved. The nanogel adjuvant can efficiently load various antigens to form a stable nano vaccine, activate an immune microenvironment and provide more means and thoughts for vaccine development.

The present invention relates to a novel immunoregulatory peptide having the ability to control inflammatory responses, and a use thereof. The peptide of the present invention may be useful in the treatment of inflammation, various immune diseases, or cancer, by regulating the activity of immune cells.

The application relates to the field of biotechnology, and particularly discloses an immunoregulatory peptide as well as a preparation method and application thereof. Three new polypeptides with ideal immunoregulatory effects are found through specific enzymolysis and screening, and the polypeptides have the amino acid sequences shown in any one or more of SEQ ID No. 1-3. The application enriches the types of milk-derived bioactive peptides, and provides new raw materials for preparing immunoregulatory effect products.

The application discloses an immunoregulatory peptide BugaCATH and application thereof, and belongs to the field of biomedicine. Buga The CATH is a cyclic polypeptide with a pair of intramolecular disulfide bond composed of a sixth cysteine and a thirteenth cysteine, and has a molecular weight of 3156.67 Dalton and an isoelectric point of 8.76, wherein the amino acid sequence is shown as SEQ ID NO: 2. Buga The gene (GenBank accession: OQ870533) of the CATH precursor is composed of 663 nucleotide sequences, and the nucleotide sequence is shown as SEQ ID NO: 1; wherein the nucleotide at the positions of 322-448 is the immunoregulatory peptide Buga The encoding gene of the CATH. The immunoregulatory peptide Buga The application of the CATH in the preparation of a treatment drug for promoting skin wound repair.

The invention belongs to the fields of traditional Chinese medicines and proteins, provides application of Xiaochaihu decoction in preparation of a medicine for treating peritoneal dialysis related peritonitis, and identifies various antibacterial and immunomodulatory peptides from the Xiaochaihu decoction. The application proves that the common goldenrop decoction has a remarkable adjuvant therapy effect on peritoneal dialysis related peritonitis, and the antibacterial and immunomodulatory polypeptide identified on the basis has remarkable antibacterial and immunomodulatory activity, so that a good basis is provided for further development of medicines.

The application provides an Euphausia superba immunomodulatory peptide, which is prepared by alkaline protease and flavour protease for enzymolysis, and then the enzymolysis product is purified by cation exchange chromatography, Sephadex G25 gel chromatography and C18 reverse phase high performance liquid chromatography. The amino acid sequence of a polypeptide is SEQ ID NO: 1 or SEQ ID NO: 2. The Euphausia superba is used as raw material, Euphausia superba peptides are obtained by enzymolysis, and the amino acid sequences of the Euphausia superba peptides are analyzed and identified by LC-MS / MS after step-by-step purification. With the help of an activity prediction tool and molecular docking, a target peptide with good immunomodulatory activity potential is screened. The target peptide is artificially synthesized, the immunomodulatory activity is verified, and the action mechanism is further clarified. Data support is provided for the prediction screening and structure-activity relationship research of Euphausia superba source high-efficiency immunomodulatory peptides.

This invention belongs to the field of food biotechnology and discloses an abalone-derived immunomodulatory peptide, its preparation method, and its application. The abalone-derived immunomodulatory peptide of this invention is obtained through a combination of dual-enzyme digestion and molecular docking screening. It includes at least one peptide with amino acid sequences as shown in SEQ ID NO. 1-6, and the docking energies with the receptor TLR4 are -7.4 kcal / mol, -6.9 kcal / mol, -6.8 kcal / mol, -6.8 kcal / mol, -6.8 kcal / mol, and -6.6 kcal / mol, respectively. Experiments have demonstrated that the above-mentioned abalone peptide possesses high immunomodulatory activity, providing a foundation for its application in the preparation of functional foods from natural food sources, and is of great significance for the development of novel immunomodulatory peptide products.

This invention specifically relates to spirulina immunomodulatory peptides, their preparation methods, and applications, belonging to the field of protein bioactive peptide technology. This invention is the first to screen immunomodulatory peptides Ser-Pro-Ser-Trp-Tyr (SPSWY), Met-Phe-Asp-Ala-Phe (MFDAF), and Phe-Gly-Arg-Phe-Arg (FGRFR) from spirulina phycocyanin. The structure and immunomodulatory activity of peptides SPSWY, MFDAF, and FGRFR were clarified. Peptides SPSWY, MFDAF, and FGRFR can enhance macrophage cell viability and phagocytic capacity, and also increase the secretion of NO and cytokines by macrophages. Their immunomodulatory activity also exhibits good stability. Furthermore, peptides SPSWY, MFDAF, and FGRFR have the advantages of being safe, non-toxic, and having high biological activity.

The present disclosure provides variant immunomodulatory polypeptides, and fusion polypeptides comprising the variant immunomodulatory peptides. The present disclosure provides T-cell modulatory multimeric polypeptides, and compositions comprising same, where the T-cell modulatory multimeric polypeptides comprise a variant immunomodulatory polypeptide of the present disclosure. The present disclosure provides nucleic acids comprising nucleotide sequences encoding the T-cell modulatory multimeric polypeptides, and host cells comprising the nucleic acids. The present disclosure provides methods of modulating the activity of a T cell; the methods comprise contacting the T cell with a T-cell modulatory multimeric polypeptide of the present disclosure.

This invention relates to the field of biomedical technology, and particularly to a process for preparing chicken thymus immunomodulatory peptides using a compound enzymatic hydrolysis method, the chicken thymus immunomodulatory peptides, and their applications. The steps are as follows: First, the chicken thymus tissue is pretreated, including thawing, cutting, microwave-assisted treatment, and high-speed homogenization. Then, pepsin pre-hydrolysis is performed, the pH is adjusted, and pepsin is added to the reaction. Next, the hydrolysis is optimized by pH gradient conversion (pH 4.8-5.2→6.3-6.7→7.3-7.7), followed by trypsin secondary hydrolysis. Then, the peptides are purified using a gradient membrane separation system (10kDa, 1kDa, 500Da), and the 1kDa-500Da fraction is collected. Finally, the collected fraction is concentrated and freeze-dried to obtain the target peptide. This process combines enzymatic hydrolysis and membrane separation technology to effectively extract highly active immunomodulatory peptides. The yield of active peptides in this invention is increased by approximately 42%, and the purity is increased by approximately 28%.

This invention belongs to the field of biotechnology, specifically relating to a highly immunomodulatory peptide derived from silkworm pupa protein, its preparation method, and its applications. The invention provides a silkworm pupa protein immunomodulatory peptide, the amino acid sequence of which is shown in SEQ ID NO.2, SEQ ID NO.3, and / or SEQ ID NO.8. This silkworm pupa protein immunomodulatory peptide is prepared by hydrolyzing silkworm pupa protein with alkaline protease, followed by purification of the enzymatic hydrolysis product through ultrafiltration and gel filtration. The most immunomodulatory peptide is screened by determining the immunomodulatory activity index, and identified by LC-MS / MS to obtain a highly immunomodulatory peptide derived from silkworm pupa protein. This immunomodulatory peptide strongly binds to TLR2 and TLR4 / MD-2 receptors through hydrogen bonds and hydrophobic interactions, activating immunity and effectively promoting macrophage proliferation and phagocytosis. This immunomodulatory peptide exhibits good immunomodulatory activity and can be used as a potential functional food ingredient.

The application discloses an immunomodulatory peptide Ha-CATH and application thereof, and belongs to the field of biomedicine. The immunomodulatory peptide Ha-CATH is a cyclic polypeptide with a pair of intramolecular disulfide bonds formed by the eighth cysteine residue and the thirteenth cysteine residue of a skin repair peptide gene of Chinese amphibian Pelophylax nigromaculatus, has a molecular weight of 2361.8 Dalton, an isoelectric point of 6.04, and an amino acid sequence shown in SEQ ID NO:1. A gene (GenBank accession: OQ992774) encoding the precursor of the immunomodulatory peptide Ha-CATH is composed of 714 nucleotides, has a nucleotide sequence shown in SEQ ID NO:2, and the nucleotide sequence of 445-504 is the encoding gene of the immunomodulatory peptide Ha-CATH. ‑ The application also discloses an application of the immunomodulatory peptide Ha-CATH in preparation of a skin wound repair promoting therapeutic drug. ‑ The application also discloses an application of the immunomodulatory peptide Ha-CATH in preparation of a skin wound repair promoting therapeutic drug.

The present disclosure provides T-cell modulatory multimeric polypeptides (T-Cell-MMP) and their epitope conjugates comprising at least one immunomodulatory polypeptide (“MOD”) that may be selected to exhibit reduced binding affinity to a cognate co-immunomodulatory polypeptide (“Co-MOD”). The epitope may be, for example, a cancer-associated epitope, an infectious disease-associated epitope, or a self-epitope. The T-Cell-MMP-epitope conjugates are useful for modulating the activity of a T-cell by delivering immunomodulatory peptides, such as IL-2 or IL-2 variants that exhibit reduced binding affinity for the IL-2R, to T-cells in an epitope selective / specific manner, and accordingly, for treating individuals with a cancer, infectious disease or autoimmune disorder.

Aspects of the present disclosure include methods for modulating macrophage activity. Methods according to certain embodiments include contacting a macrophage with a mannose receptor (CD206) binding agent in a manner sufficient to modulate activity of the macrophage. Methods for converting a phenotype of a macrophage from an M2 phenotype to an M1 phenotype are also provided. Methods for inhibiting growth of a CD206-expressing cell as well as methods for treating a subject for a neoplastic condition (e.g., cancer) or a condition associated with chronic inflammation are described. Immuno-modulating peptides suitable for use in the subject methods are also presented.

The application discloses frog meat protein source active peptides and application thereof in preparation of immunomodulators, and belongs to the technical field of active peptides. Two novel immunomodulatory peptides GIHETTYNS and IVRDIKEK are identified from the hydrolysate of Rana spinosa meat, which can significantly improve the proliferation activity of macrophage RAW264.7, accelerate the cell cycle, promote the production of NO and cytokines, and improve the level of active oxygen. The results of inflammation reaction experiments show that the active peptides can relieve inflammation. The results of molecular docking show that the active peptides are combined with the key region of TLR4 / MD-2 through hydrogen bond and hydrophobic interaction. In addition, bioinformatics analysis shows that the active peptides have good safety and stability. In summary, the active peptides are expected to become new raw materials of natural immunomodulators and anti-inflammatory agents, and promote the high-value utilization of Rana spinosa.

The application discloses a preparation method of lactoferrin immunomodulatory peptide and application thereof. The application provides recombinant escherichia coli which is escherichia coli capable of expressing fusion protein SUMO-LF(IMP); the fusion protein SUMO-LF(IMP) is fused by a SUMO tag and lactoferrin immunomodulatory peptide (SEQ ID NO:1 or SEQ ID NO:2 or SEQ ID NO:3). The recombinant strain of the application can efficiently express target protein, the expressed immunomodulatory active fragment retains natural immunomodulatory activity, and the prokaryotic expression system has the advantages of low culture cost, short fermentation period, easy separation and purification of protein and the like, the constructed strain can produce immunomodulatory active fragments on a large scale, provides a core production strain for product development in the fields of immunomodulators, biological pharmaceuticals, functional food additives and the like, and has important industrial application value and market prospect.

The invention develops a method for rapidly screening bovine colostrum immunomodulatory peptides based on DPPH free radical scavenging rate. The optimal enzymolysis conditions (alkaline protease, 5.01%, 2355.46 U / g and 4.59 h) are determined through multi-enzyme system screening and response surface optimization, and the feasibility of rapid screening based on the DPPH free radical scavenging rate is verified through correlation analysis of the DPPH free radical scavenging rate and macrophage phagocytic activity. The active peptide smaller than 3kDa is obtained through ultrafiltration and LC-MS / MS identification, the immunoregulation effect of the active peptide is remarkable, the screening efficiency is greatly improved compared with that of a traditional method, and an efficient and reliable technical scheme is provided for large-scale preparation of the food-borne immunoregulation peptide.

The application discloses a frog meat protein source active peptide with immunoregulation and anti-inflammatory functions and application thereof, and belongs to the technical field of active peptides. A novel immunoregulation peptide IADRMQKE is identified from anophrynus spinosus meat hydrolysate, which can significantly improve the proliferation activity of macrophage RAW264.7, accelerate the cell cycle, promote the production of NO and cytokines, and improve the active oxygen level. The results of inflammation reaction experiments show that the active peptide can relieve inflammation reaction. The results of molecular docking show that the active peptide is combined with the key region of TLR4 / MD-2 through hydrogen bond and hydrophobic interaction. In addition, bioinformatics analysis shows that the active peptide has good safety and stability. In summary, the active peptide is expected to become a new raw material of natural immunoregulator and anti-inflammatory agent, and promote the high-value utilization of anophrynus spinosus.

The application discloses a ternary fusion polypeptide Col-TF-1 targeting senescent cells, a matching monoclonal antibody mAb SC-1, and an anti-aging composition containing both and application. The fusion polypeptide is composed of a targeting peptide targeting a uPAR receptor on the surface of senescent cells, a collagen active peptide promoting collagen synthesis, and an immunomodulatory peptide activating NK cells through a flexible linker GGGGS, and the amino acid sequence is shown as SEQ ID NO. 1. The matching antibody mAb SC-1 is reconstructed by humanizing the CDR region and designed with a pH-sensitive histidine switch, the affinity is improved by 5 times in a slightly acidic environment, and the ADCC effect is enhanced through a fucose-deficient host cell. Experiments show that the combination of the fusion polypeptide and the antibody can make the clearance rate of senescent cells reach 45.2%, and the collagen density is improved by 83.5%, which is significantly better than the effect of a single drug. The composition provided by the application can be applied to the fields of cosmetics, medical devices, drugs and functional foods, and provides a new strategy for the treatment of aging-related diseases and the development of anti-aging products.

The invention relates to the technical field of biological medicine, in particular to a process for preparing chicken thymus immunomodulatory peptide through a compound enzymolysis method, the chicken thymus immunomodulatory peptide and application of the chicken thymus immunomodulatory peptide, and the process comprises the following steps that firstly, chicken thymus tissue is pretreated, including unfreezing, cutting, microwave-assisted treatment and high-speed homogenization, then pepsin prehydrolysis is conducted, and the chicken thymus immunomodulatory peptide is obtained; the preparation method comprises the following steps: carrying out enzymolysis and membrane separation on trypsin, adjusting the pH value, adding pepsin, carrying out a reaction, carrying out pH gradient conversion (the pH value is 4.8-5.2 to 6.3-6.7 to 7.3-7.7) to optimize hydrolysis, carrying out trypsin secondary hydrolysis, carrying out purification through a gradient membrane separation system (10kDa, 1kDa and 500Da), collecting 1kDa-500Da components, and finally concentrating and freeze-drying the collected components to obtain the target peptide. According to the process, the yield of the active peptide is increased by about 42%, and the purity of the active peptide is increased by about 28%.