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Enzymatic Fragment Condensation of Side Chain‐Protected Peptides using Subtilisin A in Anhydrous Organic Solvents: A General Strategy for Industrial Peptide Synthesis
Author(s) -
Nuijens Timo,
Schepers Annette H. M.,
Cusan Claudia,
Kruijtzer John A. W.,
Rijkers Dirk T. S.,
Liskamp Rob M. J.,
Quaedflieg Peter J. L. M.
Publication year - 2013
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201200694
Subject(s) - chemistry , anhydrous , subtilisin , side chain , dipeptide , peptide , residue (chemistry) , nucleophile , combinatorial chemistry , organic chemistry , peptide synthesis , stereochemistry , condensation , enzyme , biochemistry , catalysis , polymer , physics , thermodynamics
Herein, the enzymatic condensation of side chain‐protected peptide fragments using subtilisin A in anhydrous organic solvents is described. A screening with dipeptide Cbz‐Val‐Xxx carboxamidomethyl esters with H‐Xxx‐Val‐NH 2 nucleophiles was performed, wherein Xxx stands for every (side chain‐protected) amino acid residue. Finally, it was demonstrated that it is feasible to enzymatically condense larger peptide fragments (up to the 10‐mer level) bearing multiple side chain‐protecting groups with very high conversion.