Regioselective Hydrolysis of Human Serum Albumin by ZrIV-Substituted Polyoxotungstates at the Interface of Positively Charged Protein Surface Patches and Negatively Charged Amino Acid Residues

Complexes comprising the Lewis acidic ZrIV 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 polyoxometal...

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Veröffentlicht in:Chemistry : a European journal 2014-04, Vol.20 (14), p.3894-3897
Hauptverfasser: Stroobants, Karen, Absillis, Gregory, Moelants, Eva, Proost, Paul, Parac-Vogt, Tatjana N.
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container_issue 14
container_start_page 3894
container_title Chemistry : a European journal
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creator Stroobants, Karen
Absillis, Gregory
Moelants, Eva
Proost, Paul
Parac-Vogt, Tatjana N.
description Complexes comprising the Lewis acidic ZrIV 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. Polyoxometalates for protein hydrolysis: Complexes comprising the Lewis acidic ZrIV 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 (see illustration). Higher reactivities were found for structures with higher polyoxometalate charges and the cleavage positions were found in protein regions of mixed charge.
doi_str_mv 10.1002/chem.201303622
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subjects Chemistry
human serum albumin
hydrolysis
metalloproteases
polyoxometalates
Proteins
title Regioselective Hydrolysis of Human Serum Albumin by ZrIV-Substituted Polyoxotungstates at the Interface of Positively Charged Protein Surface Patches and Negatively Charged Amino Acid Residues
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