17 results about "Regulatory peptide" patented technology

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 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.

The present application discloses PLPC-DB, an ultrapurified phospholipoproteomic composition derived from the supernatant of peripheral blood mononuclear cells (PBMCs). It comprises essential phospholipids, bioactive proteins, regulatory peptides, and intercellular signaling factors. The composition exceeds 99% purity through a multi-stage purification process combining high-speed centrifugation and selective ultrafiltration (1-50 kDa), followed by lyophilization. This process ensures structural stability for ≥24 months and inter-batch variability <2%. PLPC-DB supports reproducibility and molecular integrity in research and diagnostic settings. Key components include phosphatidylcholine and phosphatidylserine for membrane stabilization and intracellular signaling; structural and regulatory lipids for membrane biogenesis and immune-relevant components involved in antigen presentation, cytokine modulation, and membrane-associated signaling. These may include structurally defined molecules compatible with immunological evaluation in experimental and non-therapeutic settings. The composition is formulated for bioaccessible delivery via sublingual, endonasal, transdermal, and injectable routes, and is intended exclusively for non-therapeutic use in experimental and translational models.

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.

The invention relates to the technical field of TGF-beta regulating peptides, in particular to a TGF-beta regulating peptide as well as a composition, a product and application thereof. The amino acid sequence of the TGF-beta regulating peptide disclosed by the invention comprises (a) any one of the amino acid sequences shown as SEQ ID NO. 1-SEQ ID NO. 20, (b) any one of the amino acid sequences shown as SEQ ID NO. (b) amino acid sequences which are obtained by modifying the N end and / or the C end of the TGF-beta regulating peptide limited by (a) and have the same or similar functions. The TGF-beta regulating peptide provided by the invention can effectively activate a TGF-beta / Smad signal channel, promote the synthesis of collagen and inhibit the generation of sebum, has the effects of resisting skin aging and regulating grease secretion, and has a wide application prospect in the fields of medicines, foods and cosmetics.

Disclosed are compositions and methods for a non-coding nucleic acid gene editing platform for the delivery of regulatory nucleic acid sequences and small peptides in a cell. In a particular aspect, provided herein is a non-coding nucleic acid gene editing platform to down regulate endogenous genes and genes from pests and pathogens causing diseases. In another aspect, the non-coding nucleic acid gene editing platform described herein is useful to deliver small regulatory peptides encoded from nucleic acid sequences embedded in a non-coding nucleic acid of a gene. More specifically, the non-coding nucleic acid gene editing platform provided herein allows using non-coding nucleic acid from any gene to deliver regulatory nucleic acids and small peptides in a cell. In another aspect, such regulatory nucleic acids and small peptides are useful to develop traits to enhance crop quality and yield.

The invention relates to an adiponectin receptor regulating peptide as well as a composition, a product and application thereof. The amino acid sequence of the adiponectin receptor regulating peptide is as follows: (a), any one of the amino acid sequences as shown in SEQ ID NO. 1 to 30, SEQ ID NO. 32, SEQ ID NO. 35 to 39, SEQ ID NO. 42, SEQ ID NO. 46, SEQ ID NO. 47, SEQ ID NO. 49 and SEQ ID NO. 50; or (b) any one of amino acid sequences which are obtained by modifying the N end and / or the C end of the adiponectin receptor regulating peptide limited by (a) and have the same or similar functions. The adiponectin receptor regulating peptide provided by the invention can activate an adiponectin receptor / AMPK signal channel and promote hair growth, has multiple effects of oxidation resistance, inflammation resistance and apoptosis resistance, can improve skin aging, and has wide application prospects in the fields of medicines, foods and cosmetics.

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 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 application relates to a cysteine functionalized MoS2 nanopore and application thereof in single-molecule protein and post-translational modification detection. The device realizes the regulation of the interaction between molecules in the pore, the gating state and the transport rate by constructing a peptide chain valve structure fixed by cysteine in the MoS2 nanopore and introducing positively charged and aromatic amino acids. By adjusting the composition of the peptide chain and the voltage condition, the van der Waals force, the electrostatic force and the hydrogen bond force between the protein molecule and the pore can be enhanced, the single-molecule protein can be slowly transported through the pore and the high-resolution ion current detection can be realized. The application can be used for distinguishing different amino acids, protein sequence characteristics and post-translational modification sites such as phosphorylation, and has high sensitivity, high selectivity and good scalable application prospect in protein sequencing, post-translational modification positioning and biomolecular genomics analysis.

The application discloses selective ACKR3 modulating peptides comprising amino acid sequence FGGX1MRRX2 (SEQ ID NO: 1), wherein X1 is F or W; X2 is K, V or F; and wherein the peptides have a length of at most 15 amino acids; fusion proteins comprising the peptides as taught herein; nucleic acids encoding the peptides as taught herein; nucleic acid expression cassettes and vectors comprising the nucleic acid as taught herein; and pharmaceutical compositions comprising the peptide as taught herein or the nucleic acid as taught herein. Further provided are the peptide as taught herein for use as a medicament; methods for in vitro or ex vivo diagnosis, prediction, prognosis and / or monitoring of a disease or condition characterized by an aberrant level of ACKR3 polypeptide using the peptide as taught herein; and in vitro methods for identifying an agent useful as a therapeutic using the peptide as taught herein.

The invention provides a pharmaceutical composition for treating teenager dysmenorrhea and a preparation method and application thereof, the pharmaceutical composition is prepared by compatibility of 23 traditional Chinese medicines such as cassia twig, white peony root, pollen typhae, trogopterus dung, dragon's blood and the like, and a composite regulatory peptide and a micro-ecological regulator are innovatively added. Experiments show that the composition significantly inhibits a COX-2 / PGE2 pathway and reduces the level of inflammatory factors such as IL-6 and TNF-alpha through a multi-target synergistic effect, and in an animal model, the twisting frequency is reduced by 66%, the incubation period is prolonged by 142%, the COX-2 expression is reduced by 63%, and the abundance of intestinal bifidobacterium is improved by 20%. Clinical data show that the cure rate in three menstrual cycles reaches 85%, the recurrence rate is only 5%, and the traditional Chinese medicine composition is superior to the traditional western medicine. The preparation method adopts a process of combining gradient temperature decoction with 4-6 DEG C low-temperature active ingredient addition. The ointment formulation solves the problems of poor taste and low compliance of decoction, and has no adverse effect. Traditional dysmenorrhea treatment limitation is broken through, and a safe and efficient treatment scheme is provided for primary dysmenorrhea of teenagers through a synergistic interaction mechanism of the medicines.

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%.