Anion‐regulated binding selectivity of Cr(III) in collagen
We present a mechanism for the selectivity of covalent/electrostatic binding of the Cr(III) ion to collagen, mediated by the kosmotropicity of the anions. Although a change in the long‐range ordered structure of collagen is observed after covalent binding (Cr(III)‐OOC) in the presence of SO42− at pH...
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| Veröffentlicht in: | Biopolymers 2020-11, Vol.111 (11), p.e23406-n/a |
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| container_title | Biopolymers |
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| creator | Zhang, Yi Mehta, Megha Mansel, Bradley W. Ng, Hon Wei Liu, Yang Holmes, Geoff Le Ru, Eric C. Prabakar, Sujay |
| description | We present a mechanism for the selectivity of covalent/electrostatic binding of the Cr(III) ion to collagen, mediated by the kosmotropicity of the anions. Although a change in the long‐range ordered structure of collagen is observed after covalent binding (Cr(III)‐OOC) in the presence of SO42− at pH 4.5, the νsym(COO−) band remains intense, suggesting a relatively lower propensity for the Cr(III) to bind covalently instead of electrostatically through Cr(H2O)63+. Replacing SO42− with Cl− reduces the kosmotropic effect which further favors the electrostatic binding of Cr(III) to collagen. Our findings allow a greater understanding of mechanism‐specific metal binding in the collagen molecule. We also report for the first time, surface‐enhanced Raman spectroscopy to analyze binding mechanisms in collagen, suggesting a novel way to study chemical modifications in collagen‐based biomaterials. |
| doi_str_mv | 10.1002/bip.23406 |
| format | Article |
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Although a change in the long‐range ordered structure of collagen is observed after covalent binding (Cr(III)‐OOC) in the presence of SO42− at pH 4.5, the νsym(COO−) band remains intense, suggesting a relatively lower propensity for the Cr(III) to bind covalently instead of electrostatically through Cr(H2O)63+. Replacing SO42− with Cl− reduces the kosmotropic effect which further favors the electrostatic binding of Cr(III) to collagen. Our findings allow a greater understanding of mechanism‐specific metal binding in the collagen molecule. We also report for the first time, surface‐enhanced Raman spectroscopy to analyze binding mechanisms in collagen, suggesting a novel way to study chemical modifications in collagen‐based biomaterials.</description><identifier>ISSN: 0006-3525</identifier><identifier>EISSN: 1097-0282</identifier><identifier>DOI: 10.1002/bip.23406</identifier><language>eng</language><publisher>Hoboken, USA: John Wiley & Sons, Inc</publisher><subject>Anions ; Binding ; Biomaterials ; Biomedical materials ; Chromium ; Collagen ; collagen structure ; Covalence ; covalent binding ; electrostatic interactions ; ions ; Raman spectroscopy ; Selectivity ; Trivalent chromium</subject><ispartof>Biopolymers, 2020-11, Vol.111 (11), p.e23406-n/a</ispartof><rights>2020 Wiley Periodicals LLC</rights><rights>2020 Wiley Periodicals LLC.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3676-54ecee86a9245b95d959473d8fe67cd95c5596ff81a79c77a10a678357ca2a7f3</citedby><cites>FETCH-LOGICAL-c3676-54ecee86a9245b95d959473d8fe67cd95c5596ff81a79c77a10a678357ca2a7f3</cites><orcidid>0000-0003-4371-9085 ; 0000-0002-3052-9947 ; 0000-0002-4196-3036</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fbip.23406$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fbip.23406$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,777,781,1412,27905,27906,45555,45556</link.rule.ids></links><search><creatorcontrib>Zhang, Yi</creatorcontrib><creatorcontrib>Mehta, Megha</creatorcontrib><creatorcontrib>Mansel, Bradley W.</creatorcontrib><creatorcontrib>Ng, Hon Wei</creatorcontrib><creatorcontrib>Liu, Yang</creatorcontrib><creatorcontrib>Holmes, Geoff</creatorcontrib><creatorcontrib>Le Ru, Eric C.</creatorcontrib><creatorcontrib>Prabakar, Sujay</creatorcontrib><title>Anion‐regulated binding selectivity of Cr(III) in collagen</title><title>Biopolymers</title><description>We present a mechanism for the selectivity of covalent/electrostatic binding of the Cr(III) ion to collagen, mediated by the kosmotropicity of the anions. Although a change in the long‐range ordered structure of collagen is observed after covalent binding (Cr(III)‐OOC) in the presence of SO42− at pH 4.5, the νsym(COO−) band remains intense, suggesting a relatively lower propensity for the Cr(III) to bind covalently instead of electrostatically through Cr(H2O)63+. Replacing SO42− with Cl− reduces the kosmotropic effect which further favors the electrostatic binding of Cr(III) to collagen. Our findings allow a greater understanding of mechanism‐specific metal binding in the collagen molecule. We also report for the first time, surface‐enhanced Raman spectroscopy to analyze binding mechanisms in collagen, suggesting a novel way to study chemical modifications in collagen‐based biomaterials.</description><subject>Anions</subject><subject>Binding</subject><subject>Biomaterials</subject><subject>Biomedical materials</subject><subject>Chromium</subject><subject>Collagen</subject><subject>collagen structure</subject><subject>Covalence</subject><subject>covalent binding</subject><subject>electrostatic interactions</subject><subject>ions</subject><subject>Raman spectroscopy</subject><subject>Selectivity</subject><subject>Trivalent chromium</subject><issn>0006-3525</issn><issn>1097-0282</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><recordid>eNp10MtKw0AUBuBBFKzVhW8QcNMu0p7MNQE3tXgJFHSh62E6mZQp6aTONEp3PoLP6JM4Na4EV4cD3_k5_AhdZjDJAPB0abcTTCjwIzTIoBAp4BwfowEA8JQwzE7RWQhrAEpJBgN0PXO2dV8fn96sukbtTJUsrausWyXBNEbv7Jvd7ZO2TuZ-VJblOLEu0W3TqJVx5-ikVk0wF79ziF7ubp_nD-ni8b6czxapJlzwlFGjjcm5KjBly4JVBSuoIFVeGy503DRjBa_rPFOi0EKoDBQXOWFCK6xETYZo1OduffvambCTGxu0iU8403ZBxliecwo5j_TqD123nXfxu6g4JUAEPqhxr7RvQ_CmlltvN8rvZQby0KOMPcqfHqOd9vbdNmb_P5Q35VN_8Q04FnKc</recordid><startdate>202011</startdate><enddate>202011</enddate><creator>Zhang, Yi</creator><creator>Mehta, Megha</creator><creator>Mansel, Bradley W.</creator><creator>Ng, Hon Wei</creator><creator>Liu, Yang</creator><creator>Holmes, Geoff</creator><creator>Le Ru, Eric C.</creator><creator>Prabakar, Sujay</creator><general>John Wiley & Sons, Inc</general><general>Wiley Subscription Services, Inc</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-4371-9085</orcidid><orcidid>https://orcid.org/0000-0002-3052-9947</orcidid><orcidid>https://orcid.org/0000-0002-4196-3036</orcidid></search><sort><creationdate>202011</creationdate><title>Anion‐regulated binding selectivity of Cr(III) in collagen</title><author>Zhang, Yi ; Mehta, Megha ; Mansel, Bradley W. ; Ng, Hon Wei ; Liu, Yang ; Holmes, Geoff ; Le Ru, Eric C. ; Prabakar, Sujay</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3676-54ecee86a9245b95d959473d8fe67cd95c5596ff81a79c77a10a678357ca2a7f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Anions</topic><topic>Binding</topic><topic>Biomaterials</topic><topic>Biomedical materials</topic><topic>Chromium</topic><topic>Collagen</topic><topic>collagen structure</topic><topic>Covalence</topic><topic>covalent binding</topic><topic>electrostatic interactions</topic><topic>ions</topic><topic>Raman spectroscopy</topic><topic>Selectivity</topic><topic>Trivalent chromium</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Yi</creatorcontrib><creatorcontrib>Mehta, Megha</creatorcontrib><creatorcontrib>Mansel, Bradley W.</creatorcontrib><creatorcontrib>Ng, Hon Wei</creatorcontrib><creatorcontrib>Liu, Yang</creatorcontrib><creatorcontrib>Holmes, Geoff</creatorcontrib><creatorcontrib>Le Ru, Eric C.</creatorcontrib><creatorcontrib>Prabakar, Sujay</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biopolymers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhang, Yi</au><au>Mehta, Megha</au><au>Mansel, Bradley W.</au><au>Ng, Hon Wei</au><au>Liu, Yang</au><au>Holmes, Geoff</au><au>Le Ru, Eric C.</au><au>Prabakar, Sujay</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anion‐regulated binding selectivity of Cr(III) in collagen</atitle><jtitle>Biopolymers</jtitle><date>2020-11</date><risdate>2020</risdate><volume>111</volume><issue>11</issue><spage>e23406</spage><epage>n/a</epage><pages>e23406-n/a</pages><issn>0006-3525</issn><eissn>1097-0282</eissn><abstract>We present a mechanism for the selectivity of covalent/electrostatic binding of the Cr(III) ion to collagen, mediated by the kosmotropicity of the anions. Although a change in the long‐range ordered structure of collagen is observed after covalent binding (Cr(III)‐OOC) in the presence of SO42− at pH 4.5, the νsym(COO−) band remains intense, suggesting a relatively lower propensity for the Cr(III) to bind covalently instead of electrostatically through Cr(H2O)63+. Replacing SO42− with Cl− reduces the kosmotropic effect which further favors the electrostatic binding of Cr(III) to collagen. Our findings allow a greater understanding of mechanism‐specific metal binding in the collagen molecule. We also report for the first time, surface‐enhanced Raman spectroscopy to analyze binding mechanisms in collagen, suggesting a novel way to study chemical modifications in collagen‐based biomaterials.</abstract><cop>Hoboken, USA</cop><pub>John Wiley & Sons, Inc</pub><doi>10.1002/bip.23406</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0003-4371-9085</orcidid><orcidid>https://orcid.org/0000-0002-3052-9947</orcidid><orcidid>https://orcid.org/0000-0002-4196-3036</orcidid></addata></record> |
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| source | Wiley Online Library Journals Frontfile Complete |
| subjects | Anions Binding Biomaterials Biomedical materials Chromium Collagen collagen structure Covalence covalent binding electrostatic interactions ions Raman spectroscopy Selectivity Trivalent chromium |
| title | Anion‐regulated binding selectivity of Cr(III) in collagen |
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