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 |
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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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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.</description><identifier>ISSN: 0947-6539</identifier><identifier>EISSN: 1521-3765</identifier><identifier>DOI: 10.1002/chem.201303622</identifier><identifier>CODEN: CEUJED</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Chemistry ; human serum albumin ; hydrolysis ; metalloproteases ; polyoxometalates ; Proteins</subject><ispartof>Chemistry : a European journal, 2014-04, Vol.20 (14), p.3894-3897</ispartof><rights>2014 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fchem.201303622$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fchem.201303622$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27923,27924,45573,45574</link.rule.ids></links><search><creatorcontrib>Stroobants, Karen</creatorcontrib><creatorcontrib>Absillis, Gregory</creatorcontrib><creatorcontrib>Moelants, Eva</creatorcontrib><creatorcontrib>Proost, Paul</creatorcontrib><creatorcontrib>Parac-Vogt, Tatjana N.</creatorcontrib><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</title><title>Chemistry : a European journal</title><addtitle>Chem. Eur. J</addtitle><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.</description><subject>Chemistry</subject><subject>human serum albumin</subject><subject>hydrolysis</subject><subject>metalloproteases</subject><subject>polyoxometalates</subject><subject>Proteins</subject><issn>0947-6539</issn><issn>1521-3765</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNpdkV9v0zAUxSMEEmXwyrMlnjP8J4njx1KNtVI3qhWYxItlJ9epRxpvtgPLt-Oj4aioDzxdWTq_c-71ybL3BF8SjOnH5gDHS4oJw6yi9EW2ICUlOeNV-TJbYFHwvCqZeJ29CeEBYywqxhbZnzvorAvQQxPtL0DrqfWun4INyBm0Ho9qQHvw4xEtez0e7YD0hH74zfd8P-oQbRwjtGiXEPfs4jh0IaoIAamI4gHQZojgjWpgdtu5YOeQfkKrg_LdDHoXIZnux5Nqp2I6I-FDi26hU__Jl2kBh5aNbdEdBNuOEN5mr4zqA7z7Ny-yb5-vvq7W-fbL9Wa13OYdwwXNdfoSrBjVUNZG8JYoUhGjTW2KstCYcF2KoqiZoJqzVhjOiaCVaQTlGoMy7CL7cPJ99O4p5Ub54EY_pEhJSoJLUVNWJZU4qX7bHib56O1R-UkSLOeK5FyRPFckV-urm_MrsfmJtSHC85lV_qesOOOlvL-9lltxX3yq60LesL9Ku5pG</recordid><startdate>20140401</startdate><enddate>20140401</enddate><creator>Stroobants, Karen</creator><creator>Absillis, Gregory</creator><creator>Moelants, Eva</creator><creator>Proost, Paul</creator><creator>Parac-Vogt, Tatjana N.</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>K9.</scope></search><sort><creationdate>20140401</creationdate><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</title><author>Stroobants, Karen ; Absillis, Gregory ; Moelants, Eva ; Proost, Paul ; Parac-Vogt, Tatjana N.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-g3042-b6220a32be58f97d1a161fbf8f454b017b59448392b73d9f771926fc927b0eaf3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Chemistry</topic><topic>human serum albumin</topic><topic>hydrolysis</topic><topic>metalloproteases</topic><topic>polyoxometalates</topic><topic>Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stroobants, Karen</creatorcontrib><creatorcontrib>Absillis, Gregory</creatorcontrib><creatorcontrib>Moelants, Eva</creatorcontrib><creatorcontrib>Proost, Paul</creatorcontrib><creatorcontrib>Parac-Vogt, Tatjana N.</creatorcontrib><collection>Istex</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><jtitle>Chemistry : a European journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stroobants, Karen</au><au>Absillis, Gregory</au><au>Moelants, Eva</au><au>Proost, Paul</au><au>Parac-Vogt, Tatjana N.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>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</atitle><jtitle>Chemistry : a European journal</jtitle><addtitle>Chem. Eur. J</addtitle><date>2014-04-01</date><risdate>2014</risdate><volume>20</volume><issue>14</issue><spage>3894</spage><epage>3897</epage><pages>3894-3897</pages><issn>0947-6539</issn><eissn>1521-3765</eissn><coden>CEUJED</coden><abstract>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.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><doi>10.1002/chem.201303622</doi><tpages>4</tpages></addata></record> |
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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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