Enzymatic coupling of α,α-dialkyl amino acids using inverse substrates as acyl donors

Abstract

Two series of inverse substrates, N α -Boc- α, α-dialkyl amino acid p-guanidino- and p-(guanidinomethyl)phenyl esters, were prepared as acyl donor components for enzymatic peptide synthesis. They were found to be readily coupled with amino acid p-nitroanilide to produce peptide. Streptomyces griseus trypsin was a more efficient catalyst than bovine trypsin.