[Nonspecific trypsin substrates in the enzymatic synthesis of peptides].

Trypsin--catalyzed coupling of peptide segments in aqueous medium was studied. Carboxamido methyl esters (Cam esters) of peptides were used as acyl donors. Peptide segments involved in the coupling do not contain positively charged residues (Lys, Arg).

Protease-catalyzed peptide synthesis using inverse substrates: the synthesis of Pro-Xaa-bonds by trypsin.

Benzyloxycarbonyl-L-proline p-guanidinophenyl ester is an "inverse substrate" for trypsin; i.e., the cationic center is included in the leaving group instead of being in the acyl moiety.

Protease-catalyzed peptide synthesis using inverse substrates: the influence of reaction conditions on the trypsin acyl transfer efficiency.

Benzyloxycarbonyl-L-alanine p-guanidinophenyl ester behaves as a trypsin "inverse substrate," i.e., a cationic center is included in the leaving group instead of being in the acyl moiety.

New approaches to peptide synthesis with the help of trypsin.

Picolyl esters of amino acids are suitable inverse substrates for trypsin. These esters can be used for peptide synthesis catalyzed by trypsin. Study of hydrolysis of non-specific substrates for trypsin permits to conclude, that hydrogen band in P'2 subsite is very important for their reactivity.

Thio-alpha-amino acids (S-acids) as a carboxyl component in peptide synthesis catalysed by papain.

Peptide synthesis catalysed by papain was studied using thio-alpha-amino acids (S-acids) as a carboxyl component. It was found, for example, that with Z-AlaSH (pK 2.70) the maximal yield of the peptide Z-AlaValNH2 was obtained at pH 8-8.