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Native chemical ligation with N α acyl transfer auxiliaries
Author(s) -
Offer John
Publication year - 2010
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.21455
Subject(s) - native chemical ligation , chemistry , chemical ligation , ligation , thioester , cysteine , combinatorial chemistry , peptide , amino acid , biochemistry , stereochemistry , microbiology and biotechnology , biology , enzyme
Abstract Native chemical ligation (NCL) is a simple procedure that enables synthetic access to many proteins and is increasingly harnessed to study protein structure and function. However, the generality of this method is limited by the requirement for cysteine residues suitably positioned throughout the target protein. Auxiliary approaches have been developed to overcome this limitation, wherein a removable group is introduced at the amino terminus of a peptide conveying ligation properties comparable to cysteine. Present auxiliary approaches combine the thioester exchange concept applied first in NCL with a number of acyl transfer reactions first systematically explored by Kemp and coworkers. The current methods for auxiliary mediated ligation appear promising for the synthesis of proteins and in particular post‐translational modified proteins. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 94: 530–541, 2010.