16875-11-9

Basic information

• Product Name: PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG
• Synonyms: BRADYKININ, FRAGMENT 2-9;BRADYKININ (2-9);(DES-ARG1)-BRADYKININ;H-PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG-OH;PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG;PPGFSPFR;1-DE-L-ARGININE-BRADYKININ;L-Pro-L-Pro-Gly-L-Phe-L-Ser-L-Pro-L-Phe-L-Arg-OH
• CAS NO: 16875-11-9
• Molecular Formula: C₄₄H₆₁N₁₁O₁₀
• Molecular Weight: 904.02
• Product Categories: Peptide;BradykininsPeptides and Proteins;Bradykinins;Neuropeptides;Peptides for Cell Biology
• Mol File: 16875-11-9.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Density: 1.47 g/cm³
• Refractive Index: 1.684
• Storage Temp.: −20°C
• PKA: 3.34±0.10(Predicted)
• CAS DataBase Reference: PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG(CAS DataBase Reference)
• NIST Chemistry Reference: PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG(16875-11-9)
• EPA Substance Registry System: PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG(16875-11-9)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 16875-11-9(Hazardous Substances Data)

Usage

General Description

The chemical PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG is a peptide composed of eight amino acids in the sequence proline-proline-glycine-phenylalanine-serine-proline-phenylalanine-arginine. This sequence contributes to the formation and structure of proteins in the body, as amino acids are the building blocks of proteins. Each amino acid in the sequence plays a specific role in the function of the resulting peptide. For example, proline is known for its rigidity and ability to stabilize the structure of proteins, while phenylalanine is important for its aromatic nature and influence on protein folding. The arrangement of these different amino acids in the peptide sequence determines its biological activity and function within the body.

InChI:InChI=1/C44H61N11O10/c45-44(46)48-20-8-16-30(43(64)65)51-38(59)32(24-28-13-5-2-6-14-28)52-40(61)35-18-10-22-55(35)42(63)33(26-56)53-37(58)31(23-27-11-3-1-4-12-27)50-36(57)25-49-39(60)34-17-9-21-54(34)41(62)29-15-7-19-47-29/h1-6,11-14,29-35,47,56H,7-10,15-26H2,(H,49,60)(H,50,57)(H,51,59)(H,52,61)(H,53,58)(H,64,65)(H4,45,46,48)

Upstream product

• 58-82-2 bradykinin 

Downstream Products

• 1208549-10-3 C₆₀H₇₉N₁₃O₁₄S 

Relevant articles and documents

Inhibition and metal ion activation of pig kidney aminopeptidase P. Dependence on nature of substrate

Pig kidney aminopeptidase P (AP-P; EC 3.4.11.9) has been purified to homogeneity after its solubilisation from brush border membranes by phosphatidylinositol-specific phospholipase C. The effects of various activators and inhibitors of AP-P activity have been examined with a number of different substrates for the enzyme. The hydrolysis of bradykinin and ArgProPro is inhibited at Mn2+ concentrations above 10-5 M, whereas the hydrolysis of other substrates (GlyProHyp, β-casomorphin, substance P) is substantially activated, with 4-10 mM Mn2+ being optimal. The thiol reagent, p-chloromercuriphenylsulphonic acid, inhibits the hydrolysis of GlyProHyp but markedly activates the hydrolysis of bradykinin. A number of inhibitors of angiotensin converting enzyme (ACE; EC 3.4.15.1), previously reported to inhibit the hydrolysis of GlyProHyp, have no effect on the hydrolysis of bradykinin except in the presence of Mn2+. Differences were also observed in the degree of inhibition of GlyProHyp and bradykinin hydrolysis by EDTA and their reactivation by divalent cations. The hydrolysis of GlyProHyp follows Michaelis-Menten kinetics with a K(m) value of 2.7 mM. Bradykinin inhibits GlyProHyp hydrolysis with an I50 of 1.4 μM. The hydrolysis of bradykinin by AP-P reveals anomalous nonlinear kinetics indicative of negative cooperativity or the presence of more than one active site for this substrate. These results indicate that substrates for AP-P can be divided into 2 groups based on their responses to inhibitors and cation activators.