A novel strategy in kinetically controlled enzymatic peptide synthesis is described. Various
amino acid derivatives with charged, highly solubilizing Nα-protecting groups were prepared …

Several amino acid derivatives with the negatively charged N alpha-protecting groups
Maleyl (Mal) and Citraconyl (Cit) were synthesized and used in enzyme-catalyzed peptide …

Studies of the kinetics of peptide synthesis catalysed by trypsin derivatives have been
carried out. We have studied equilibrium (ECS) and kinetically (KCS) controlled synthesis …

An effective method for enzyme solubility-controlled synthesis of peptides, consisting in an
iterative addition of equivalent amounts of acyl and amine components to a solution …

Optimal conditions were found, for enzymatic synthesis of the dipeptide, N-acetyl-L-
tryptophanyl-L-leucine amide in the biphasic system water-ethyl acetate. The synthesis was …

Chemoenzymatic peptide synthesis is a rapidly developing technology for cost effective
peptide production on a large scale. As an alternative to the traditional C→ N strategy, which …

By using very active and very stable trypsin agarose derivatives, we have optimized the
design of the synthesis of a model dipeptide, benzoylarginine leucinamide, by two different …

In the kinetically controlled approach of peptide synthesis mediated by α-chymotrypsin, the
broadening of the protease's substrate tolerance is achieved by switching the acyl donor …

Synthesis of dipeptides benzoyl Arginine leucinamide and kyotorphin catalyzed by highly
stabilized derivatives of trypsin and chymotrypsin have been performed. Extreme …

Recently we have demonstrated the advantage of solid‐phase substrate pools mainly in
equilibrium controlled protease‐catalysed peptide syntheses. The extension of this …