14517-44-3 Usage
General Description
H-MET-GLU-OH, also known as N-methyl-L-glutamic acid, is a synthetic peptide derivative. It consists of N-methylated L-glutamic acid, an amino acid that plays a crucial role in protein synthesis and neurotransmission. The N-methylation of the glutamic acid moiety in H-MET-GLU-OH has been found to enhance the stability and conformational properties of the peptide, making it a useful tool in the study of protein structure and function. Additionally, H-MET-GLU-OH and its derivatives have shown potential therapeutic applications in the treatment of central nervous system disorders and neurodegenerative diseases.
Check Digit Verification of cas no
The CAS Registry Mumber 14517-44-3 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 1,4,5,1 and 7 respectively; the second part has 2 digits, 4 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 14517-44:
(7*1)+(6*4)+(5*5)+(4*1)+(3*7)+(2*4)+(1*4)=93
93 % 10 = 3
So 14517-44-3 is a valid CAS Registry Number.
14517-44-3Relevant articles and documents
Studies of the aminopeptidase proteolysis of semax analogues with different N-terminal amino acid residues
Shevchenko,V'yunova,Nagaev,Andreeva,Alfeeva,Myasoedov
, p. 421 - 427 (2011)
Proteolysis of semax (Met-Glu-His-Phe-Pro-Gly-Pro, Sem) and its analogues with the substitution of Ala, Gly, Thr, or Trp for the N-terminal Met was studied. This substitution was shown to change the degradation rate of these peptides by leucine aminopeptidase (EC 3.4.11.2, Sigma, Type VI, 9.2 activity units/mg). [Ala1]Sem, [Gly1]Sem, and [Thr1]Sem (the semax analogues) proved to be more stable to the proteolysis than semax itself. It was demonstrated that the primary product of the proteolysis was His-Phe-Pro-Gly-Pro (Sem-5). In the case of [Trp1]Sem, the comparable amount of Glu-His-Phe-Pro-Gly-Pro (Sem-6) was found to be formed along with Sem-5. In was established that all the studied semax analogues could be used as inhibitors of its proteolysis. Pleiades Publishing, Ltd., 2011.