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Serine‐Protease‐Assisted Synthesis of Peptide Substrates for α‐Chymotrypsin
Author(s) -
Bizzozero Spartaco A.,
Rovagnati Bruno A.,
Dutler Hans
Publication year - 1982
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19820650605
Subject(s) - chemistry , peptide , chymotrypsin , serine , amino acid , stereochemistry , peptide bond , peptide synthesis , serine protease , protease , amino acid residue , enzyme , combinatorial chemistry , peptide sequence , biochemistry , trypsin , gene
δ‐Chymotraypsin catalyzes peptide‐bond formation between acylated amino‐acid and peptide esters as the carboxyl component and amino‐acid and peptide amides as the amino component. The conditions under which enzyme‐catalyzed coupling can be used for fragment condensation in peptide synthesis is investigated. To illustrate the method the synthesis of tetra‐, penta‐ and hexapeptides of the structure Ac‐L xn … L xl L yl … L ym NH 2 with L xl Tyr, designed as substrates for α‐chymotrypsin, is described.