title: 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.
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.
authors.affiliation: Department of Chemistry, KU Leuven, Celestijnenlaan 200F, 3001 Leuven (Belgium).
authors.forename: Karen
authors.initials: K
authors.lastname: Stroobants
authors.forename: Gregory
authors.initials: G
authors.lastname: Absillis
authors.forename: Eva
authors.initials: E
authors.lastname: Moelants
authors.forename: Paul
authors.initials: P
authors.lastname: Proost
authors.forename: Tatjana N
authors.initials: TN
authors.lastname: Parac-Vogt
mesh_terms: D000596:Amino Acids; D006801:Humans; D006868:Hydrolysis; D008958:Models, Molecular; D012709:Serum Albumin / Q000737:chemistry*; D013237:Stereoisomerism; D017973:Tungsten Compounds / Q000138:chemical synthesis / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D012709:Serum Albumin; D017973:Tungsten Compounds
keywords: human serum albumin; hydrolysis; metalloproteases; polyoxometalates