153247-47-3

Basic information

• Product Name: H-VAL-VAL-PHE-OH
• Synonyms: H-VAL-VAL-PHE-OH
• CAS NO: 153247-47-3
• Molecular Formula: C19H29N3O4
• Molecular Weight: 363.45
• Mol File: 153247-47-3.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-VAL-VAL-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-VAL-VAL-PHE-OH(153247-47-3)
• EPA Substance Registry System: H-VAL-VAL-PHE-OH(153247-47-3)

Safety Data

• Hazardous Substances Data: 153247-47-3(Hazardous Substances Data)

Usage

Description

H-VAL-VAL-PHE-OH is a peptide chemical compound composed of the amino acids valine, valine, phenylalanine, and a C-terminal hydroxyl group. It is known for its potential role in muscle tissue repair and growth due to the presence of valine, an essential amino acid. Phenylalanine, another component of this peptide, is vital for the synthesis of neurotransmitters such as dopamine, norepinephrine, and epinephrine. H-VAL-VAL-PHE-OH holds promise in medicinal chemistry for its potential use in developing new pharmaceutical drugs and as a research tool for understanding protein structure and function. Furthermore, it may offer skin-soothing properties, making it a candidate for cosmetic and skincare product formulations.

Uses

Used in Pharmaceutical Industry:
H-VAL-VAL-PHE-OH is used as a building block for the development of new pharmaceutical drugs, leveraging its amino acid composition to target specific biological pathways and mechanisms.
Used in Research and Development:
H-VAL-VAL-PHE-OH serves as a research tool for studying protein structure and function, providing insights into the interactions between amino acids and their roles in biological systems.
Used in Cosmetic and Skincare Industry:
H-VAL-VAL-PHE-OH is used as an ingredient in cosmetic and skincare products for its potential skin-soothing properties, contributing to the development of formulations that promote skin health and well-being.

Relevant 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

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.