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153247-47-3

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153247-47-3 Usage

General Description

H-VAL-VAL-PHE-OH is a peptide chemical compound consisting of the amino acids valine, valine, phenylalanine, and a C-terminal hydroxyl group. Valine is an essential amino acid that plays a crucial role in muscle tissue repair and growth, while phenylalanine is needed for the synthesis of dopamine, norepinephrine, and epinephrine. This peptide may have potential applications in the field of medicinal chemistry, including as a building block for the development of new pharmaceutical drugs or as a research tool for studying protein structure and function. Additionally, it could also be used in the production of cosmetic and skincare products due to its potential skin-soothing properties.

Check Digit Verification of cas no

The CAS Registry Mumber 153247-47-3 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,5,3,2,4 and 7 respectively; the second part has 2 digits, 4 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 153247-47:
(8*1)+(7*5)+(6*3)+(5*2)+(4*4)+(3*7)+(2*4)+(1*7)=123
123 % 10 = 3
So 153247-47-3 is a valid CAS Registry Number.

153247-47-3Upstream product

153247-47-3Downstream Products

153247-47-3Relevant articles and documents

Cathepsin D activity and selectivity in the acidic conditions of a tumor microenvironment: Utilization in the development of a novel Cathepsin D substrate for simultaneous cancer diagnosis and therapy

Achour, Oussama,Bridiau, Nicolas,Kacem, Meriem,Delatouche, Régis,Bordenave-Juchereau, Stéphanie,Sannier, Frédéric,Thiéry, Valérie,Piot, Jean-Marie,Maugard, Thierry,Arnaudin, Ingrid

, p. 2010 - 2017 (2013)

Pro-Cathepsin D (pCD) is an aspartyl endopeptidase which is over expressed in many cancers. This over expression generally led to its secretion into the extracellular culture medium of cancer cells. Moreover, pCD can auto activate and cleave its substrates at an acidic pH compatible with that found in tumor microenvironments (TME). Thus, exploiting these two pathological characteristics of TME offers the opportunity to develop new protease-activated vector on the basis of their specific substrate structures. The aim of this study was to validate new pCD substrates in the extracellular pH conditions of TME. As a first step, we investigated the effect of pH on the catalytic activity and selectivity of mature Cathepsin D (CD). It was found that the increase in the pH of the media led to a decrease in the reaction rate. However, the specificity of mature CD was not affected by a variation in pH. In the second step, the effect of the substrate structure was studied. We demonstrated that the substrate structure had a significant effect on the catalytic activity of CD. In fact, some modifications in peptide structure induced a change in the catalytic behavior that involved a substrate activation phenomenon. We suggest that this activation may be related to the amphiphilic nature of the modified peptide that may induce an interfacial activation mechanism. Finally, pCD, which is the major form found in the extracellular culture medium of cancer cells, was used. We demonstrated that the proform of CD cleave the modified peptide 5 at pH 6.5 with the same cleavage selectivity obtained with the mature form of the protease. These data provide a better understanding of CD behavior in tumor microenvironment conditions and this knowledge can be used to develop more specific tools for diagnosis and drug delivery.

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