44 results about "Peptide Synthesis technique" patented technology

The invention relates to the technical field of polypeptide synthesis, and particularly relates to a solid synthetic method of semaglutide. The solid synthetic method includes coupling Gly and a resin to obtain a Gly-resin; coupling step by step for the first time an ammonia acid or an amino acid derivative to obtain a first peptide resin the sequence of which is shown as SEQ ID No.1; removing a side chain protective group of Lys; coupling step by step for a second time 2-(2-(2-aminoethoxy)ethoxy) acetic acid, 2-(2-(2-aminoethoxy)ethoxy) acetic acid, Glu and octadecanedioic acid to obtain a second peptide resin; performing pyrolysis; and purifying. The solid synthetic method is simplified in operation step, short in synthetic period, low in cost, reduced in production of waste liquid, low in side products and high in product yield, and is suitable for large-scale production of the semaglutide.

The invention provides a method for preparing thymosin alpha 1 by liquid phase fragment condensation, belonging to the technical field of biochemistry. According to the method, high capacity value (not less than 0.8mmol / g) resin is used as a starting material, firstly, a standard solid phase polypeptide synthesis (SPPS) technology is adopted for synthesizing a high-purity peptide fragments with selected structures, then, a liquid phase condensation technology is adopted for connecting the peptide fragments, and thus, a high-purity (more than 99%) target peptide is obtained. Compared with the solid phase thymosin alpha 1 synthesis technology, the method provided by the invention avoids the problem of low coupling ratio of amino acids behind the 12th position, and greatly improves yield (up to 25-30%) of the thymosin alpha 1; meanwhile, the peptide fragment formed by solid phase synthesis is free from purification, post-treatment technology is simplified, finally, the thymosin alpha 1 is purified by means of high performance liquid chromatography, preparation difficulty is reduced, preparation times is decreased, synthesis cost of the thymosin alpha 1 is lowered, and implementation of large-scale and industrialized production is facilitated.

[Problem] To provide a heretofore completely different and novel peptide synthesis technique, and to provide a novel compound that enables the synthesis / creation of a novel artificial functional protein and the synthesis / creation of a novel functional peptide, as well as a production method for said compound. [Solution] A compound represented by formula (I) or a salt thereof.

The invention relates to the technical field of amino acid polypeptide synthesis, and discloses an amino acid N-methylation synthesis method, and a product and an application thereof. According to the invention, through benzyl protection upon the carboxyl group of amino acid and through trifluoroacetyl protection upon the amino group, N-methylated amino acid can be obtained after methylation. The N-methyl(trifluoroacetyl)-amino acid benzyl ester prepared by the method provided by the invention can be directly used in polypeptide synthesis, such that an amino acid benzyl ester product with an N-methyl structure can be obtained. Also, the compound has good deprotection selectivity, and selective deprotection can be carried out upon the N-terminal and the C-terminal. Compared to a Ag2O / CH3I / Boc method (high toxicity and high cost) and a NaH / (CH3O)2SO2 method (high toxicity) abroad, the method provided by the invention has high yield. With the use of nontoxic reagents, the method is safe and nontoxic, and has the advantages of simple operation, common and easy-to-obtain raw material reagents, low cost, and high structural selectivity. The obtained product has low racemization possibility. The method has a good industrial prospect.

The invention relates to the technical field of polypeptide synthesis, in particular to a preparation method of pexiganan. The preparation method comprises the following specific steps: A) synthesizing a dipeptide fragment FmoC-Lys (BoC)-Lys (BoC)-OH by a liquid phase method; B) by a solid-phase synthesis method, with amino resin as starting resin, sequentially coupling amino acids with FmoC protections at N terminals and side chain protections according to a peptide sequence of a main chain of the pexiganan, wherein the amino acids at 7 and 8 positions, the amino acids 10 and 11 positions and the amino acids at 21 and 22 positions are coupled by the dipeptide fragment FmoC-Lys (BoC)-Lys (BoC)-OH; C) cracking, purifying and freeze-drying peptide resin to obtain the pexiganan. The invention provides a synthesis process of the pexiganan, which is high in synthesis efficiency and low in cost, can avoid deleted peptide impurities caused by incomplete coupling of two lysines and is suitable for mass production.

The invention relates to a G protein competitive inhibitory peptide, which starts from a 55 peptide sequence and obtains a series of derived polypeptides by deleting amino acid residues in any numbermore than one in any point from the first amino acid residue at the amino end and at least remaining twelve amino acid residues at the amino end. The length of the polypeptide is shortened up to 78.2percent; and the polypeptide has a remarkable effect on anti-myocardial remodelling. The invention also relates to a method for preparing the series of derived polypeptides, which successfully synthesizes a target polypeptide with the purity up to 99.2 percent by utilizing advanced peptide synthesis technology. The invention further relates to the preparations containing the polypeptides and the application thereof in the preparation of an anti-myocardial remodelling medicament.

The antibacterial peptide HP10 of the present invention and its preparation method and application belong to the technical field of peptide synthesis containing 5-20 amino acids and the specific therapeutic activity technical field of compounds and pharmaceutical preparations. The amino acid sequence of the antimicrobial peptide HP10 is HHHLHHIHKP; its molecular weight is 1292.4Da, and its isoelectric point is 8.79. Its preparation comprises the following steps: (1), the antibacterial peptide HP10 that amino acid sequence is HHHLHHIHKP is activated and cross-linked one by one from C-terminus to N-terminus by FMOC protection synthetic method; (2), the product of step (1) is subjected to HPLC Antimicrobial peptide HP10 was obtained by desalting and purification by reverse phase column chromatography. The antimicrobial peptide HP10 in the present invention has the advantages of small molecular weight, convenient artificial synthesis, strong thermal stability, strong bactericidal effect, and no drug resistance; it also has the advantages of significantly improving the intestinal health of piglets and strengthening the body when applied in piglet feed. Advantages of immunity, improving piglet growth performance.

A method for synthesizing phenylalanyl-lysine dipeptide belongs to the technical field of peptide synthesis. The invention uses commercially available phenylalanine and lysine as raw materials, prepares ethylene glycol non-aqueous reaction medium by preparing phenylalanine and lysine aqueous solution, and prepares phenylalanyl-lysine dipeptide reaction liquid , prepare a resin column for purifying loaded phenylalanyl-lysine dipeptide, prepare phenylalanyl-lysine dipeptide eluate, prepare phenylalanyl-lysine dipeptide freeze-dried powder, prepare recovery The phenylalanine and lysine aqueous solution and the step of preparing the regenerated resin column just prepare the phenylalanyl-lysine dipeptide with a content of 95-98%. The present invention uses chymotrypsin as a catalyst to synthesize phenylalanyl-lysine dipeptide in an ethylene glycol non-aqueous medium, the conditions are mild, the specificity is strong, and the synthesis efficiency is high, which is a typical green production process; the prepared Phenylalanyl-lysine dipeptide can be widely used in medicine, textile, food and other fields, and has considerable social value.