[Proteolysis of semax analogues with different N-terminal amino acids by aminopeptidases]

Autor: K V, Shevchenko, T V, V'iunova, I Iu, Nagaev, L A, Andreeva, L Iu, Alfeeva, N F, Miasoedov
Rok vydání: 2011
Předmět:
Zdroj: Bioorganicheskaia khimiia. 37(4)
ISSN: 0132-3423
Popis: Proteolysis of semax (Met-Glu-His-Phe-Pro-Gly-Pro, Sem) and its analogues ([Ala1]Sem, [Gly1]Sem, [Thr1]Sem, [Trp1]Sem) that are differ from semax in substitution of N-terminal Met residue were studied. It is shown that such replacement changes the rate of peptides degradation by N-aminopeptidases (EC 3.4.11.2, Sigma, Type VI, 9.2 units. Akt. / mg). [Ala1]Sem, [Gly1]Sem and [Thr1]Sem semax analogues proved to be more stable to proteolysis than semax (Sem), and their initial product of proteolysis is His-Phe-Pro-Gly-Pro (Sem-5). For triptophan analogue both Glu-His-Phe-Pro-Gly-Pro (Sem-6) and Sem-5 product are formed in similar quantities. It is found that all investigated analogues can be used as inhibitors in Sem proteolysis.
Databáze: OpenAIRE