16875-11-9

Usage

Uses

Used in Pharmaceutical Industry:
PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG is used as a therapeutic agent for its potential role in modulating protein structures and functions, which can be beneficial in treating various diseases and conditions related to protein misfolding or instability.
Used in Research and Development:
In the field of biotechnology and molecular biology, PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG serves as a valuable research tool for studying protein folding, stability, and interactions. It can be utilized to investigate the effects of specific amino acid sequences on protein conformation and function, contributing to a better understanding of protein biology and the development of novel therapeutic strategies.
Used in Drug Design and Development:
The unique sequence of PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG can be employed in the design of peptide-based drugs, where its specific properties can be harnessed to target particular biological pathways or receptors. This can lead to the development of more effective and targeted treatments for various diseases.
Used in Cosmetics and Skincare Industry:
Due to its influence on protein folding and stability, PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG can be used in cosmetic and skincare products to promote skin health and elasticity. Its potential to modulate protein structure may contribute to the development of anti-aging products or treatments for skin conditions related to protein misfolding or instability.
Used in Food and Nutrition Industry:
PRO-PRO-GLY-PHE-SER-PRO-PHE-ARG may find applications in the food and nutrition industry, where its role in protein structure and function can be leveraged to improve the nutritional value, texture, or stability of food products. It could be used as an ingredient in protein-enriched foods or supplements to support muscle growth and maintenance.

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 academic research and scientific papers

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.