The enzymatic segment condensation of peptides on a solid phase in organicmedium

The segment condensation of peptides on a solid phase (Aminosilochrom) in o rganic medium catalyzed by a subtilisin complex with sodium dodecylsulfate was studied. The dependence of the efficiency of the enzymatic coupling of tripeptides with the basic structure X-Ala-Ala-Y-OMe [where X = Z, Boc, or Drip and Y = Leu or Glu(OMe)] on the spacer (Phe-Met-Gly-Gly) content on th e support and on the structure of the acylating component was investigated. The tripeptide segments were successively coupled to Aminosilochrom contai ning the Met-Ala-Gly spacer, and the peptidylaminosilochroms Dnp-Ala-Ala-Le u-Ala-Ala-Leu-Ala-Ala-Glu(OMe)-Met-Ala-Gly-A and Dnp-Ala-Ala-Leu-Ala-Ala-Gl u(OMe)-Ala-Ala-Leu-Met-Ala-Gly-A (A is the Aminosilochrom residue) were obt ained in satisfactory yields. It was shown by these examples that the secon d and third segments are attached in yields higher than that for the first segment and the coupling efficiency does not depend on the amino acid compo sition of the acylating component.