23815-89-6

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Uses

Biologically active fragment of bradykinin

Biochem/physiol Actions

The bradykinin (BK) fragment (1-5) (RPPGF) is among the most stable of naturally occurring metabolites. It may be used as a marker for BK production in vivo. It is known that an intact Arg residue in the C-terminus is required for biological activities. BK 1-5 is the minimal peptide that inhibited α-thrombin-induced platelet aggregation and secretion and calcium mobilization. It also prevented α-thrombin from cleaving the thrombin receptor peptide, NATLDPRSFLLR, between arginine and serine. Such antithrombin activities of BK 1-5 may contribute to the cardioprotective nature of kinins.

InChI:InChI=1/C27H40N8O6/c28-18(9-4-12-31-27(29)30)24(38)35-14-6-11-21(35)25(39)34-13-5-10-20(34)23(37)32-16-22(36)33-19(26(40)41)15-17-7-2-1-3-8-17/h1-3,7-8,18-21H,4-6,9-16,28H2,(H,32,37)(H,33,36)(H,40,41)(H4,29,30,31)/t18-,19-,20-,21-/m0/s1

Upstream product

• 58-82-2 bradykinin 

Relevant academic research and scientific papers

Scandium(III) triflate-promoted serine/threonine-selective peptide bond cleavage

The site-selective cleavage of peptide bonds is an important chemical modification that is useful not only for the structural determination of peptides, but also as an artificial modulator of peptide/protein function and properties. Here we report site-selective hydrolysis of peptide bonds at the Ser and Thr positions with a high conversion yield. This chemical cleavage relies on Sc(iii)-promoted N,O-acyl rearrangement and subsequent hydrolysis. The method is applicable to a broad scope of polypeptides with various functional groups, including a post-translationally modified peptide that is unsuitable for enzymatic hydrolysis. The system was further extended to site-selective cleavage of a native protein, Aβ1-42, which is closely related to the onset of Alzheimer's disease.

SPECIFICITY AND MOLECULAR PROPERTIES OF PENICILLOLYSIN, A METALLOPROTEINASE FROM PENICILLUM CITRINUM

The specificity and mode of action of penicillolysin, a metalloproteinase from Penicillum citrinum, were investigated with several bioactive-oligopeptides.The enzyme showed a high affinity toward the Pro-X (X = Gln, Lys, Leu or Arg) bonds of substance P, dynorphin A (1-13), neurotensin and chicken brain pentapeptide, and the R-R bonds in dynorphin A and neurotensin.Preferential cleavages of bonds by the enzyme with hydrophobic amino acid residues at the P1 position were observed on the peptides used.The specificity of penicillolysin differs from that of other metallopropteinases.The Mr and pI were determined as 18000 and 9.6, respectively.The first 50 amino acids in the N-terminal region were TKETCSNASRKSALEKALSNTVKLANAAATAARSGSASKFSEYEKTTSSS.CD spectra on the hollo- and apo-enzymes of penicillolysin were studied.