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A Chemical Approach to Immunoprotein Engineering: Chemoselective Functionalization of Thioester Proteins in Their Native State
Author(s) -
Cole Michael A.,
Tully Sarah E.,
Dodds Alister W.,
Arnold James N.,
Boldt Grant E.,
Sim Robert B.,
Offer John,
Wentworth Paul
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200900168
Subject(s) - thioester , chemistry , native chemical ligation , hydrazide , hydrolysis , surface modification , stereochemistry , combinatorial chemistry , biochemistry , organic chemistry , cysteine , enzyme
Less than 6 feet under : Serum proteins C3, C4, and α 2 M each contain a thioester domain buried within a hydrophobic pocket, which is thought to shield the labile thioester from hydrolysis. Herein, we make use of the inherent reactivity of the hydrazide for thioester moieties to chemoselectively label these crucial serum regulators in their native conformation; this demonstrates that access to the thioester site is much greater than previously supposed.