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Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity
The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings’ capacity to bind antithrombin. Current methods for accelerated life-time testing are based on exposing leaflets to water solutions....
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Published in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2006-04, Vol.49 (1), p.1-7 |
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creator | Kristensen, E.M.E. Larsson, R. Sánchez, J. Rensmo, H. Gelius, U. Siegbahn, H. |
description | The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings’ capacity to bind antithrombin. Current methods for accelerated life-time testing are based on exposing leaflets to water solutions. In this paper a method is explored, in which heart valve leaflets were exposed to a continuous high shear rate (4
L/min) of human citrated plasma. It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma. It was, however, partly destroyed by the test as found using XPS. We suggest that heparin chains from the upper layer of heparin have been torn off from the carrier chain, in combination with loss of heparin conjugate and plasma deposition in patches. This study showed that XPS provides additional information to biological measurements such as antithrombin uptake. XPS is therefore a valuable technique not only to characterize biomaterials but also to evaluate the effect of a performance test. |
doi_str_mv | 10.1016/j.colsurfb.2006.02.007 |
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L/min) of human citrated plasma. It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma. It was, however, partly destroyed by the test as found using XPS. We suggest that heparin chains from the upper layer of heparin have been torn off from the carrier chain, in combination with loss of heparin conjugate and plasma deposition in patches. This study showed that XPS provides additional information to biological measurements such as antithrombin uptake. XPS is therefore a valuable technique not only to characterize biomaterials but also to evaluate the effect of a performance test.</description><identifier>ISSN: 0927-7765</identifier><identifier>ISSN: 1873-4367</identifier><identifier>EISSN: 1873-4367</identifier><identifier>DOI: 10.1016/j.colsurfb.2006.02.007</identifier><identifier>PMID: 16567083</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Antithrombins - chemistry ; Antithrombins - metabolism ; Antithrombins/chemistry/metabolism ; Biocompatibility ; Biocompatible Materials - chemistry ; Carbohydrate Conformation ; Carbohydrate Sequence ; Chemistry ; Electrons ; Heart valve ; Heart Valves - chemistry ; Heart Valves - metabolism ; Heart Valves/chemistry/metabolism ; Heparin - chemistry ; Humans ; Immobilized heparin ; Kemi ; Materials Testing ; MEDICIN ; MEDICINE ; Molecular Sequence Data ; Photoelectron spectroscopy ; Sensitivity and Specificity ; Spectrum Analysis ; Surface characterization ; Surface Properties ; X-Rays</subject><ispartof>Colloids and surfaces, B, Biointerfaces, 2006-04, Vol.49 (1), p.1-7</ispartof><rights>2006 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-f88ce49f963adcbe8bd70915fb8b9ea36ae19da27581a1d068c406b9c702c9423</citedby><cites>FETCH-LOGICAL-c433t-f88ce49f963adcbe8bd70915fb8b9ea36ae19da27581a1d068c406b9c702c9423</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16567083$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-94387$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Kristensen, E.M.E.</creatorcontrib><creatorcontrib>Larsson, R.</creatorcontrib><creatorcontrib>Sánchez, J.</creatorcontrib><creatorcontrib>Rensmo, H.</creatorcontrib><creatorcontrib>Gelius, U.</creatorcontrib><creatorcontrib>Siegbahn, H.</creatorcontrib><title>Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity</title><title>Colloids and surfaces, B, Biointerfaces</title><addtitle>Colloids Surf B Biointerfaces</addtitle><description>The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings’ capacity to bind antithrombin. Current methods for accelerated life-time testing are based on exposing leaflets to water solutions. In this paper a method is explored, in which heart valve leaflets were exposed to a continuous high shear rate (4
L/min) of human citrated plasma. It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma. It was, however, partly destroyed by the test as found using XPS. We suggest that heparin chains from the upper layer of heparin have been torn off from the carrier chain, in combination with loss of heparin conjugate and plasma deposition in patches. This study showed that XPS provides additional information to biological measurements such as antithrombin uptake. XPS is therefore a valuable technique not only to characterize biomaterials but also to evaluate the effect of a performance test.</description><subject>Antithrombins - chemistry</subject><subject>Antithrombins - metabolism</subject><subject>Antithrombins/chemistry/metabolism</subject><subject>Biocompatibility</subject><subject>Biocompatible Materials - chemistry</subject><subject>Carbohydrate Conformation</subject><subject>Carbohydrate Sequence</subject><subject>Chemistry</subject><subject>Electrons</subject><subject>Heart valve</subject><subject>Heart Valves - chemistry</subject><subject>Heart Valves - metabolism</subject><subject>Heart Valves/chemistry/metabolism</subject><subject>Heparin - chemistry</subject><subject>Humans</subject><subject>Immobilized heparin</subject><subject>Kemi</subject><subject>Materials Testing</subject><subject>MEDICIN</subject><subject>MEDICINE</subject><subject>Molecular Sequence Data</subject><subject>Photoelectron spectroscopy</subject><subject>Sensitivity and Specificity</subject><subject>Spectrum Analysis</subject><subject>Surface characterization</subject><subject>Surface Properties</subject><subject>X-Rays</subject><issn>0927-7765</issn><issn>1873-4367</issn><issn>1873-4367</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhi1ERZeFv1D5xAUl2HHijxtVCxSpUisVEDfLH5PWq2wc7GTR_nu82gWOPYwsS888M5oXoQtKakoo_7CpXRzyknpbN4TwmjQ1IeIFWlEpWNUyLl6iFVGNqITg3Tl6nfOGENK0VLxC55R3XBDJVqi_gcmkMGIXzRzGR-yXZGwYwrzHccQmzaEPLpgBP0H54J0ZdpBxnhcfwGO7xz_vH7AZfak5zE8pbm2xlfIHmzOTccX1Bp31Zsjw9vSu0ffPn75d3VS3d1--Xl3eVq5lbK56KR20qlecGe8sSOsFUbTrrbQKDOMGqPKmEZ2khnrCpWsJt8oJ0jjVNmyN3h-9-TdMi9VTCluT9jqaoK_Dj0sd06NeFq1aVu60Ru-O9JTirwXyrLchOxgGM0JcsuZC0UZJ8ixIi091TBaQH0GXYs4J-n8bUKIPwemN_hucPgSnSaNLcKXx4jRhsVvw_9tOSRXg4xGAcr5dgKSzCzA68CGBm7WP4bkZfwCt0K9N</recordid><startdate>20060415</startdate><enddate>20060415</enddate><creator>Kristensen, E.M.E.</creator><creator>Larsson, R.</creator><creator>Sánchez, J.</creator><creator>Rensmo, H.</creator><creator>Gelius, U.</creator><creator>Siegbahn, H.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>DF2</scope></search><sort><creationdate>20060415</creationdate><title>Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity</title><author>Kristensen, E.M.E. ; Larsson, R. ; Sánchez, J. ; Rensmo, H. ; Gelius, U. ; Siegbahn, H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-f88ce49f963adcbe8bd70915fb8b9ea36ae19da27581a1d068c406b9c702c9423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Antithrombins - chemistry</topic><topic>Antithrombins - metabolism</topic><topic>Antithrombins/chemistry/metabolism</topic><topic>Biocompatibility</topic><topic>Biocompatible Materials - chemistry</topic><topic>Carbohydrate Conformation</topic><topic>Carbohydrate Sequence</topic><topic>Chemistry</topic><topic>Electrons</topic><topic>Heart valve</topic><topic>Heart Valves - chemistry</topic><topic>Heart Valves - metabolism</topic><topic>Heart Valves/chemistry/metabolism</topic><topic>Heparin - chemistry</topic><topic>Humans</topic><topic>Immobilized heparin</topic><topic>Kemi</topic><topic>Materials Testing</topic><topic>MEDICIN</topic><topic>MEDICINE</topic><topic>Molecular Sequence Data</topic><topic>Photoelectron spectroscopy</topic><topic>Sensitivity and Specificity</topic><topic>Spectrum Analysis</topic><topic>Surface characterization</topic><topic>Surface Properties</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kristensen, E.M.E.</creatorcontrib><creatorcontrib>Larsson, R.</creatorcontrib><creatorcontrib>Sánchez, J.</creatorcontrib><creatorcontrib>Rensmo, H.</creatorcontrib><creatorcontrib>Gelius, U.</creatorcontrib><creatorcontrib>Siegbahn, H.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Uppsala universitet</collection><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kristensen, E.M.E.</au><au>Larsson, R.</au><au>Sánchez, J.</au><au>Rensmo, H.</au><au>Gelius, U.</au><au>Siegbahn, H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity</atitle><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle><addtitle>Colloids Surf B Biointerfaces</addtitle><date>2006-04-15</date><risdate>2006</risdate><volume>49</volume><issue>1</issue><spage>1</spage><epage>7</epage><pages>1-7</pages><issn>0927-7765</issn><issn>1873-4367</issn><eissn>1873-4367</eissn><abstract>The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings’ capacity to bind antithrombin. Current methods for accelerated life-time testing are based on exposing leaflets to water solutions. In this paper a method is explored, in which heart valve leaflets were exposed to a continuous high shear rate (4
L/min) of human citrated plasma. It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma. It was, however, partly destroyed by the test as found using XPS. We suggest that heparin chains from the upper layer of heparin have been torn off from the carrier chain, in combination with loss of heparin conjugate and plasma deposition in patches. This study showed that XPS provides additional information to biological measurements such as antithrombin uptake. XPS is therefore a valuable technique not only to characterize biomaterials but also to evaluate the effect of a performance test.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>16567083</pmid><doi>10.1016/j.colsurfb.2006.02.007</doi><tpages>7</tpages></addata></record> |
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subjects | Antithrombins - chemistry Antithrombins - metabolism Antithrombins/chemistry/metabolism Biocompatibility Biocompatible Materials - chemistry Carbohydrate Conformation Carbohydrate Sequence Chemistry Electrons Heart valve Heart Valves - chemistry Heart Valves - metabolism Heart Valves/chemistry/metabolism Heparin - chemistry Humans Immobilized heparin Kemi Materials Testing MEDICIN MEDICINE Molecular Sequence Data Photoelectron spectroscopy Sensitivity and Specificity Spectrum Analysis Surface characterization Surface Properties X-Rays |
title | Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity |
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