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Highly Amino Acid Selective Hydrolysis of Myoglobin at Aspartate Residues as Promoted by Zirconium(IV)‐Substituted Polyoxometalates
Author(s) -
Ly Hong Giang T.,
Absillis Gregory,
Janssens Rik,
Proost Paul,
ParacVogt Tatja.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201502006
Subject(s) - hydrolysis , myoglobin , chemistry , edman degradation , zirconium , peptide , cleavage (geology) , selectivity , peptide bond , residue (chemistry) , organic chemistry , chromatography , peptide sequence , biochemistry , catalysis , materials science , fracture (geology) , gene , composite material
SDS‐PAGE/Edman degradation and HPLC MS/MS showed that zirconium(IV)‐substituted Lindqvist‐, Keggin‐, and Wells–Dawson‐type polyoxometalates (POMs) selectively hydrolyze the protein myoglobin at AspX peptide bonds under mildly acidic and neutral conditions. This transformation is the first example of highly sequence selective protein hydrolysis by POMs, a novel class of protein‐hydrolyzing agents. The selectivity is directed by Asp residues located on the surface of the protein and is further assisted by electrostatic interactions between the negatively charged POMs and positively charged surface patches in the vicinity of the cleavage site.