8 results about "Core peptide" patented technology

The invention belongs to the technical field of plant peptide preparation, and particularly relates to a preparation method of pea oligopeptide and application of the pea oligopeptide in the aspect of reducing blood sugar. The pea oligopeptide is prepared by taking pea protein as a raw material through an enzymolysis method, core peptide fragments VA, FPW and WPF of the pea oligopeptide are obtained through further identification on the basis, and VA, FPW and WPF are screened and confirmed as potential inhibitory peptides targeting DPP-IV by combining molecular docking and molecular dynamics simulation technologies. Besides, the DPP-IV inhibition rate of the core peptide fragment is further determined through an in-vitro experiment, and the FPW and the WPF are confirmed to be the core peptide fragment with efficient DPP-IV inhibition potential and have relatively good structural stability by combining cell experiment analysis, so that theoretical support is provided for the hypoglycemic effect of the pea peptide core peptide fragment, and a foundation is laid for development of hypoglycemic nutritional and healthy products.

The application discloses a plant selenoprotein enzyme peptide composition, effervescent tablets and application thereof, and relates to the field of functional food, and comprises the following components in parts by weight: selenium-rich shepherd's purse powder 5-12 parts; comprehensive fruit and vegetable fermentation powder 8-15 parts; soybean peptide powder 3-10 parts; comprehensive digestive enzyme 05-3 parts; and pharmaceutically or dietetically acceptable excipients; the plant selenoprotein enzyme peptide composition, the effervescent tablets and the application thereof are scientifically combined with organic selenium (selenium-rich shepherd's purse powder), active enzymes and small-molecule metabolites generated by fermentation of various fruits and vegetables, soybean peptides easy to absorb and prebiotics. Selenium is the core of the antioxidant system, peptides and fermentation products provide nutritional substrates and regulatory signals, prebiotics improve the intestinal microenvironment, and multiple components synergistically act on multiple pathways such as immunity and metabolism.

The invention belongs to the technical field of bioactive peptides, and particularly relates to a cyperus esculentus-derived DPP-IV inhibitory peptide as well as a preparation method and application thereof. The DPP-IV inhibitory peptide has good in-vivo hypoglycemic activity, through screening and identification, the core peptide fragment comprises YLFPGFG, FGHPEW, VLPPPW and the like, the three oligopeptides have high DPP-IV inhibitory activity, the IC50 values of the three oligopeptides are 0.5047 mM, 1.199 mM and 1.596 mM respectively, all the oligopeptides are competitive inhibition, and the DPP-IV inhibitory peptide can be used as a DPP-IV natural inhibitory peptide with low side effects and good curative effects and has good application prospects. The method has important theoretical and practical significance for early prevention of diabetes mellitus.

An object is to provide a peptide gelling agent which gels under physiological conditions and which has a relatively short chain length, and a sustained-release gel based on the gelling agent. A hydrogelling self-assembling peptide is provided having one or two core peptides with an amino acid sequence of the formula: Xaa-Yaa-Zaa-Yaa-Xaa-Yaa-Zaa-Yaa-Xaa, wherein Xaa is independently Ile or Met, Yaa is independently Asp, Glu, Lys, or Arg, and Zaa is independently Ala or Gly. The full length of the amino acid sequence constituting the self-assembling peptide is 25 amino acids or less.

The present invention relates to novel albumin binding constructs that enhance the pharmacokinetic performance of therapeutic peptides and proteins, extend their half-life and reduce the frequency of administration. The core peptide DICLPRWGCLW (SEQ ID NO: 1) is covalently linked to a hydrophilic and flexible glycine-serine (Gly-Ser) linker of the formula (ggs) xg, wherein x is from 3 to 8 units. The linkers provide a strong binding force (dissociation constant lt; 20 nanomoles) to albumin. Some constructs have a GGSGGSGGSGGRLIEDICLPRGCLWEDD (SEQ ID NO: 4) peptide, allowing fusion of active proteins, such as Klotho, maintaining biological activity, and utilizing the long half-life of albumin. In some embodiments, constructs are produced using cellular expression systems (CHO cells, HEK293 cells, transgenic insect cells) to ensure scalability. Upon administration, these constructs exhibit an extended half-life up to at least 90% of the half-life of native albumin. The novel Klotho constructs using the novel albumin conjugates show a FGF23 binding dissociation constant of from 15 to 30 nanomoles, substantially the same as that of natural Klotho. These constructs are designed to minimize antigenicity, thereby enhancing drug delivery effectiveness and improving patient prognosis.

The invention belongs to the technical field of fusion protein, and particularly relates to a semeglutide precursor polypeptide and a semeglutide preparation process. The precursor polypeptide provided by the invention is a fusion protein containing the semeglutide and comprises a virus-like particle protein (seq), a protease specific recognition sequence and a semeglutide core 29 peptide (SEQ ID NO: 1), and the fusion protein forms 60 poly virus-like particles. The virus-like particles are subjected to graded ammonium sulfate precipitation purification and heating to remove other proteins of thalli, soluble components are collected to obtain the virus-like particles containing the precursor polypeptide of the semeglutide, the virus-like particles are removed through enterokinase digestion and ultrafiltration, and the high-purity semeglutide can be obtained. The method is simple in purification step, and the production cost is reduced.

The application relates to the field of biological information and discloses a toxic protein library construction method, device, equipment and medium. The method comprises the following steps: acquiring a common peptide structure corresponding to a confirmed toxic protein sequence, and constructing a target toxic protein core peptide set capable of covering a key functional domain of the confirmed toxic protein sequence based on function performance characteristic data and fluctuation trend characteristic data of the common peptide structure. The target toxic protein core peptide set is used for function screening of a to-be-recognized protein sequence in a function characteristic domain, so that an intermediate protein sequence needing to be verified whether it meets a toxicity characteristic is obtained, toxicity screening of the intermediate protein sequence in a toxicity characteristic domain is performed, and the intermediate protein sequence meeting the toxicity characteristic is determined as a target toxic protein sequence. Finally, a toxic protein database is constructed by using the target toxic protein sequence. Thus, a toxic protein library construction method with a wide coverage range which can discover new toxic proteins and detect low-abundance toxic proteins is realized through a two-level screening mode combining function screening and toxicity screening.

The application belongs to the technical field of fusion proteins, and particularly relates to a semaglutide precursor polypeptide and a semaglutide preparation process. The precursor polypeptide provided by the application is a fusion protein containing semaglutide, which comprises a virus-like particle protein (seq), a protease-specific recognition sequence and a semaglutide core 29 peptide (SEQ ID NO: 1). The fusion protein forms a 60-polymer virus-like particle. The virus-like particle is purified by fractional ammonium sulfate precipitation, heated to remove bacteria and other proteins, and the soluble components are collected to obtain a virus-like particle containing the semaglutide precursor polypeptide. The virus-like particle is subjected to enterokinase digestion, and the virus-like particle is removed by ultrafiltration, so that high-purity semaglutide is obtained. The method has simple purification steps and reduces production costs.