223271-86-1Relevant academic research and scientific papers
Synthesis of new chromogenic substrates for aspartyl proteases
Litvinova,Balandina,Stepanov
, p. 7 - 11 (2007/10/03)
A general method was developed for the synthesis of new chromogenic substrates of aspartyl proteases: Dnp-Ala-Xaa-Phe-Phe-Ala-Arg-NH2, where Xaa was Ala or Ser. The synthetic scheme involved both chemical and enzymic stages, the condensation of tripeptides in an organic medium by means of pepsin immobilized on Celite being among the latters. The influence of organic solvents, reaction time, and the composition and ionic strength of the buffers used in the reaction mixture and at the pepsin immobilization step on the efficacy of the pepsin-catalyzed synthesis was studied.
Enzymatic Synthesis of Arginine-Containing Peptides - Chromophore Substrates of Metalloproteinases and Carbopeptidases
Yusupova, M. P.,Kotlova, E. K.,Timokhina, E. A.,Stepanov, V. M.
, p. 27 - 32 (2007/10/02)
Subtilisin 72 sorbed on the surface of macroporous glass catalyzes condensation of N-acylated peptide esters with arginine derivatives in organic solvents.The sorbed enzyme can be used repeatedly, which makes it possible to synthesize the chromophore substrates of metalloproteinases and carbopeptidases with the general formula Dnp-Ala-Ala-Xaa-Arg-NH2 (Xaa = Leu, Phe, Val, Ile).In the tetrapeptides, metalloproteinases hydrolyze the Ala-Xaa bond and cleave off Dnp-Ala-Ala-OH, which can be determined spectrophotometrically.The chromophore substrates of B type carboxypeptidases (Dnp-Ala-Ala-Xaa-Arg-OH and Dnp-Ala-Ala-Arg-OH) are obtained by hydrolysis of the corresponding amides with trypsin. Key words: enzymatic synthesis, subtilisin, chromophore substrate, metalloproteinase.
