92411-00-2

Upstream product

• 16652-71-4 benzyl (2S)-2-pyrrolidinecarboxylate hydrochloride 
• 51785-82-1 N-tert-butyloxycarbonyl-L-prolylglycine 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 57294-31-2 tert-butyl (S)-2-((2-ethoxy-2-oxoethyl)carbamoyl)pyrrolidine-1-carboxylate 
• 83610-54-2 glycyl-L-proline benzyl ester trifluoroacetate 

Downstream Products

• 7561-51-5 Pro-Gly-Pro 
• 92411-05-7 Boc-Met-γ-Bzl-Glu-His-Phe-Pro-Gly-Pro-OBzl 
• 80714-61-0 H-Met-Glu-His-Phe-Pro-Gly-Pro 
• 92411-04-6 Boc-γ-Bzl-Glu-His-Phe-Pro-Gly-Pro-OBzl 
• 92411-06-8 Boc-Met-Glu-His-Phe-Pro-Gly-Pro 
• 92411-03-5 Boc-His-Phe-Pro-Gly-Pro-OBzl 

Relevant academic research and scientific papers

METHOD FOR PRODUCING RECOMBINANT PEPTIDE AND RESULTANT PEPTIDE

PROBLEM TO BE SOLVED: To provide peptides with reproductive- and sexual-function stimulating activity. SOLUTION: The peptides are represented by general formula: A-Thr-Lys-Pro-B-C-D-X (where A is 0, Met, Met(O), Thr, Ala, His, Phe, Lys, or Gly; B is 0, Gly, Asp, Trp, Gln, Asn, Tyr, Pro, or Arg; C is 0, Arg, Phe, Tyr, Gly, His, Pro, or Lys; D is 0, Val, Gly, Tyr, Trp, Phe, or His; and X is OH, OCH3, or NH2; where 0 represents absence of the amino acid residue; provided that if A≠0 then B ≠0 and/or C≠0 and/or D≠0, if B≠0 then C≠0 and/or D≠0, and peptides Phe-Thr-Lys-Pro-Gly, Thr-Lys-Pro-Pro-Arg and Thr-Lys-Pro-Arg-Gly are excluded). SELECTED DRAWING: Figure 1 COPYRIGHT: (C)2020,JPO&INPIT

Method for producing a recombinant peptide and resultant peptide

The invention relates to peptides with the following general formula: [in-line-formulae]A-Thr-Lys-Pro-B-C-D-X, where:[/in-line-formulae] A—0, Met, Met (O), Thr, Ala, His, Phe, Lys, Gly B—0, Gly, Asp, Trp, Gln, Asn, Tyr, Pro, Arg C—0, Arg, Phe, Tyr, Gly, His, Pro, Lys D—0, Val, Gly, Tyr, Trp, Phe, His X—OH, OCH3, NH2, where 0 is no amino acid residue, provided that if A≠0, then B and/or C and/or D≠0, if B≠0, then C and/or D≠0, excluding the peptides Phe-Thr-Lys-Pro-Gly (SEQ ID NO: 1), Thr-Lys-Pro-Pro-Arg (SEQ ID NO: 2), Thr-Lys-Pro-Arg-Gly (SEQ ID NO: 3).

Stability of His-Phe-Arg-Trp-Pro-Gly-Pro to Leucine Aminopeptidase, Carboxypeptidase Y, and Rat Nasal Mucus, Blood, and Plasma

The His-Phe-Arg-Trp-Pro-Gly-Pro [ACTH-(6-9)-PGP] peptide was synthesized. Proteolysis of ACTH-(6-9)-PGP and semax (Met-Glu-His-Phe-Pro-Gly-Pro) in the presence of leucine aminopeptidase and carboxypeptidase Y was studied. If the proteolysis of ACTH-(6-9)-PGP is mainly defined by aminopeptidases, the basic metabolite is Trp-Pro-Gly-Pro. Identification of major metabolites of ACTH-(6-9)PGP when incubated with the enzymes in vitro made it possible to evaluate proteolysis pathways of the peptide and prepare necessary amounts of its metabolites for using them as standards. Kinetics of ACTH-(6-9)PGP degradation in the presence of enzyme systems of nasal mucus, blood, and plasma were also explored. It was found that proteolysis of ACTH-(6-9)-PGP in rat blood and plasma occurs mainly under the effect of enzymes whose action is similar to leucine aminopeptidase.

Structural-functional study of glycine-and-proline-containing peptides (Glyprolines) as potential neuroprotectors

A synthetic scheme for preparation of (Gly-Pro) n, (Pro-Gly) n (n = 2, 3), and (Pro-Gly-Pro) n (n = 1, 2) peptides was elaborated. The effect of the synthesized peptides and the Gly-Pro and Pro-Gly dipeptides on survival of cultured cells of PC12 rat pheochromocytoma was studied under the conditions of oxidative stress induced by brief incubation of the cells with hydrogen peroxide. Peptides of the general formula (Gly-Pro) n and the Pro-Gly-Pro peptide at a concentration of 0.2-100 μM were shown to decrease the number of damaged cells. The Gly-Pro peptide was the most active and decreased the number of damaged cells by 49% on average at a concentration of 100 μM.