150114-97-9 Usage
Uses
Used in Pharmaceutical Development:
Fmoc-Val-Ala-OH is used as a building block for the synthesis of bioactive peptides for various therapeutic applications. Its role in solid-phase peptide synthesis allows for the creation of peptides with specific sequences that can target diseases or conditions, offering potential treatments and interventions.
Used in Scientific Research:
Fmoc-Val-Ala-OH is used as a component in the study of peptide structure, function, and interactions with other biomolecules. Researchers utilize Fmoc-Val-Ala-OH to investigate the properties of peptides and their potential roles in biological processes, contributing to a deeper understanding of peptide-based mechanisms in health and disease.
Used in Drug Design and Discovery:
Fmoc-Val-Ala-OH is used as a key component in the design and discovery of new drugs. Its incorporation into peptides allows for the exploration of novel therapeutic agents with specific activities, selectivity, and pharmacokinetic properties, advancing the development of innovative medications for various diseases and disorders.
Check Digit Verification of cas no
The CAS Registry Mumber 150114-97-9 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,5,0,1,1 and 4 respectively; the second part has 2 digits, 9 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 150114-97:
(8*1)+(7*5)+(6*0)+(5*1)+(4*1)+(3*4)+(2*9)+(1*7)=89
89 % 10 = 9
So 150114-97-9 is a valid CAS Registry Number.
150114-97-9Relevant articles and documents
Glutamic Acid Selective Chemical Cleavage of Peptide Bonds
Nalbone, Joseph M.,Lahankar, Neelam,Buissereth, Lyssa,Raj, Monika
supporting information, p. 1186 - 1189 (2016/03/15)
Site-specific hydrolysis of peptide bonds at glutamic acid under neutral aqueous conditions is reported. The method relies on the activation of the backbone amide chain at glutamic acid by the formation of a pyroglutamyl (pGlu) imide moiety. This activation increases the susceptibility of a peptide bond toward hydrolysis. The method is highly specific and demonstrates broad substrate scope including cleavage of various bioactive peptides with unnatural amino acid residues, which are unsuitable substrates for enzymatic hydrolysis.