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Regioselective Hydrolysis of Human Serum Albumin by Zr IV ‐Substituted Polyoxotungstates at the Interface of Positively Charged Protein Surface Patches and Negatively Charged Amino Acid Residues
Author(s) -
Stroobants Karen,
Absillis Gregory,
Moelants Eva,
Proost Paul,
ParacVogt Tatja.
Publication year - 2014
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201303622
Subject(s) - polyoxometalate , chemistry , human serum albumin , cleavage (geology) , hydrolysis , reactivity (psychology) , regioselectivity , lewis acids and bases , amino acid , metal , electrostatics , crystallography , stereochemistry , medicinal chemistry , inorganic chemistry , organic chemistry , biochemistry , catalysis , materials science , medicine , alternative medicine , pathology , fracture (geology) , composite material
Abstract Complexes comprising the Lewis acidic Zr IV metal and protein binding polyoxotungstate ligands of Lindqvist‐, Keggin‐ and Wells–Dawson‐type were found to region selectively hydrolyze human serum albumin at four distinct positions. Higher reactivities were found for structures with higher polyoxometalate charges and the cleavage positions were found in protein regions of mixed charge. Both findings suggest an electrostatic nature of the observed reactivity.