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Proteins at polysaccharide-based biointerfaces: A comparative study of QCM-D and electrokinetic measurements
Controlling protein adsorption on biomaterial surfaces requires a thorough understanding of interfacial phenomena. Proteins adhering after implantation influence successful biointegration. Deciphering adsorption mechanisms at biointerfaces is crucial and of high interest. Here, a combination of time...
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Published in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2023-01, Vol.221, p.113011-113011, Article 113011 |
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description | Controlling protein adsorption on biomaterial surfaces requires a thorough understanding of interfacial phenomena. Proteins adhering after implantation influence successful biointegration. Deciphering adsorption mechanisms at biointerfaces is crucial and of high interest. Here, a combination of time-resolved in situ electrokinetic measurements and quartz crystal microbalance with dissipation monitoring (QCM-D) was employed to understand the adsorption phenomena of blood proteins at thin layers of polysaccharide-based biointerfaces. Adsorption kinetics of bovine serum albumin (BSA), fibrinogen (Fg), and γ-globulin (γG) was studied on polydimethylsiloxane (PDMS) coatings functionalised with chitosan-surfactant complex and hyaluronic acid. The functionalised surfaces show a suppressed protein affinity compared to hydrophobic PDMS. Fg exhibits peculiar adsorption behaviour on PDMS, stemming from the highly oriented end-on adsorption with freely moving α chains. BSA demonstrates arbitrary surface orientation, while γG shows preferential surface orientation on PDMS, exposing a higher density of cationic moieties. The combination of the mentioned techniques proved beneficial for the investigation of interactions, orientations, and changes at biointerfaces in real-time. The approach is versatile and promising where research on surfaces and interfaces is in high demand.
[Display omitted]
•BSA, Fg, and γG adsorption near physiological conditions on different surfaces.•Investigation of interactions, orientations, and changes at biointerfaces.•Comparison of results from QCM-D and electrokinetic measurements.•Highly oriented end-on adsorption of Fg on PDMS with freely moving α chains. |
doi_str_mv | 10.1016/j.colsurfb.2022.113011 |
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[Display omitted]
•BSA, Fg, and γG adsorption near physiological conditions on different surfaces.•Investigation of interactions, orientations, and changes at biointerfaces.•Comparison of results from QCM-D and electrokinetic measurements.•Highly oriented end-on adsorption of Fg on PDMS with freely moving α chains.</description><identifier>ISSN: 0927-7765</identifier><identifier>EISSN: 1873-4367</identifier><identifier>DOI: 10.1016/j.colsurfb.2022.113011</identifier><language>eng</language><publisher>Elsevier B.V</publisher><subject>adsorption ; biocompatible materials ; blood ; bovine serum albumin ; comparative study ; Electrokinetic measurements ; Fibrinogen ; hyaluronic acid ; hydrophobicity ; polydimethylsiloxane ; Protein adsorption ; QCM-D ; quartz crystal microbalance ; Serum albumin ; γ-globulin</subject><ispartof>Colloids and surfaces, B, Biointerfaces, 2023-01, Vol.221, p.113011-113011, Article 113011</ispartof><rights>2022 Elsevier B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c308t-625a98b379e75bee324cb85a6bbb93406bd2c123a4c632c207b0106f9a4a63353</citedby><cites>FETCH-LOGICAL-c308t-625a98b379e75bee324cb85a6bbb93406bd2c123a4c632c207b0106f9a4a63353</cites><orcidid>0000-0001-6053-6294</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27907,27908</link.rule.ids></links><search><creatorcontrib>Ajdnik, Urban</creatorcontrib><creatorcontrib>Luxbacher, Thomas</creatorcontrib><creatorcontrib>Fras Zemljič, Lidija</creatorcontrib><title>Proteins at polysaccharide-based biointerfaces: A comparative study of QCM-D and electrokinetic measurements</title><title>Colloids and surfaces, B, Biointerfaces</title><description>Controlling protein adsorption on biomaterial surfaces requires a thorough understanding of interfacial phenomena. Proteins adhering after implantation influence successful biointegration. Deciphering adsorption mechanisms at biointerfaces is crucial and of high interest. Here, a combination of time-resolved in situ electrokinetic measurements and quartz crystal microbalance with dissipation monitoring (QCM-D) was employed to understand the adsorption phenomena of blood proteins at thin layers of polysaccharide-based biointerfaces. Adsorption kinetics of bovine serum albumin (BSA), fibrinogen (Fg), and γ-globulin (γG) was studied on polydimethylsiloxane (PDMS) coatings functionalised with chitosan-surfactant complex and hyaluronic acid. The functionalised surfaces show a suppressed protein affinity compared to hydrophobic PDMS. Fg exhibits peculiar adsorption behaviour on PDMS, stemming from the highly oriented end-on adsorption with freely moving α chains. BSA demonstrates arbitrary surface orientation, while γG shows preferential surface orientation on PDMS, exposing a higher density of cationic moieties. The combination of the mentioned techniques proved beneficial for the investigation of interactions, orientations, and changes at biointerfaces in real-time. The approach is versatile and promising where research on surfaces and interfaces is in high demand.
[Display omitted]
•BSA, Fg, and γG adsorption near physiological conditions on different surfaces.•Investigation of interactions, orientations, and changes at biointerfaces.•Comparison of results from QCM-D and electrokinetic measurements.•Highly oriented end-on adsorption of Fg on PDMS with freely moving α chains.</description><subject>adsorption</subject><subject>biocompatible materials</subject><subject>blood</subject><subject>bovine serum albumin</subject><subject>comparative study</subject><subject>Electrokinetic measurements</subject><subject>Fibrinogen</subject><subject>hyaluronic acid</subject><subject>hydrophobicity</subject><subject>polydimethylsiloxane</subject><subject>Protein adsorption</subject><subject>QCM-D</subject><subject>quartz crystal microbalance</subject><subject>Serum albumin</subject><subject>γ-globulin</subject><issn>0927-7765</issn><issn>1873-4367</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><recordid>eNqFkU9P3DAUxK2KSizbfgXkYy_Z-l_shFPRAi3SVgWpPVvPzovqJYkX20Hab9-gLWdO7zIzmjc_Qi4523DG9df9xschz6l3G8GE2HAuGecfyIo3RlZKanNGVqwVpjJG1-fkIuc9Y0woblZkeEixYJgyhUIPcThm8P4vpNBh5SBjR12IYSqYevCYr-g19XE8QIISXpDmMndHGnv6uP1Z3VCYOooD-pLiU5iwBE9HhKUbjjiV_Il87GHI-Pn_XZM_d7e_tz-q3a_v99vrXeUla0qlRQ1t46Rp0dQOUQrlXVODds61UjHtOuG5kKC8lsILZhzjTPctKNBS1nJNvpxyDyk-z5iLHUP2OAwwYZyzlbyWDVeNUe9KhZGNapedxSLVJ6lPMeeEvT2kMEI6Ws7sKwm7t28k7CsJeyKxGL-djLj8_BIw2ewDTh67kJatbBfDexH_AKhclc0</recordid><startdate>202301</startdate><enddate>202301</enddate><creator>Ajdnik, Urban</creator><creator>Luxbacher, Thomas</creator><creator>Fras Zemljič, Lidija</creator><general>Elsevier B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><orcidid>https://orcid.org/0000-0001-6053-6294</orcidid></search><sort><creationdate>202301</creationdate><title>Proteins at polysaccharide-based biointerfaces: A comparative study of QCM-D and electrokinetic measurements</title><author>Ajdnik, Urban ; Luxbacher, Thomas ; Fras Zemljič, Lidija</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c308t-625a98b379e75bee324cb85a6bbb93406bd2c123a4c632c207b0106f9a4a63353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>adsorption</topic><topic>biocompatible materials</topic><topic>blood</topic><topic>bovine serum albumin</topic><topic>comparative study</topic><topic>Electrokinetic measurements</topic><topic>Fibrinogen</topic><topic>hyaluronic acid</topic><topic>hydrophobicity</topic><topic>polydimethylsiloxane</topic><topic>Protein adsorption</topic><topic>QCM-D</topic><topic>quartz crystal microbalance</topic><topic>Serum albumin</topic><topic>γ-globulin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ajdnik, Urban</creatorcontrib><creatorcontrib>Luxbacher, Thomas</creatorcontrib><creatorcontrib>Fras Zemljič, Lidija</creatorcontrib><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ajdnik, Urban</au><au>Luxbacher, Thomas</au><au>Fras Zemljič, Lidija</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Proteins at polysaccharide-based biointerfaces: A comparative study of QCM-D and electrokinetic measurements</atitle><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle><date>2023-01</date><risdate>2023</risdate><volume>221</volume><spage>113011</spage><epage>113011</epage><pages>113011-113011</pages><artnum>113011</artnum><issn>0927-7765</issn><eissn>1873-4367</eissn><abstract>Controlling protein adsorption on biomaterial surfaces requires a thorough understanding of interfacial phenomena. Proteins adhering after implantation influence successful biointegration. Deciphering adsorption mechanisms at biointerfaces is crucial and of high interest. Here, a combination of time-resolved in situ electrokinetic measurements and quartz crystal microbalance with dissipation monitoring (QCM-D) was employed to understand the adsorption phenomena of blood proteins at thin layers of polysaccharide-based biointerfaces. Adsorption kinetics of bovine serum albumin (BSA), fibrinogen (Fg), and γ-globulin (γG) was studied on polydimethylsiloxane (PDMS) coatings functionalised with chitosan-surfactant complex and hyaluronic acid. The functionalised surfaces show a suppressed protein affinity compared to hydrophobic PDMS. Fg exhibits peculiar adsorption behaviour on PDMS, stemming from the highly oriented end-on adsorption with freely moving α chains. BSA demonstrates arbitrary surface orientation, while γG shows preferential surface orientation on PDMS, exposing a higher density of cationic moieties. The combination of the mentioned techniques proved beneficial for the investigation of interactions, orientations, and changes at biointerfaces in real-time. The approach is versatile and promising where research on surfaces and interfaces is in high demand.
[Display omitted]
•BSA, Fg, and γG adsorption near physiological conditions on different surfaces.•Investigation of interactions, orientations, and changes at biointerfaces.•Comparison of results from QCM-D and electrokinetic measurements.•Highly oriented end-on adsorption of Fg on PDMS with freely moving α chains.</abstract><pub>Elsevier B.V</pub><doi>10.1016/j.colsurfb.2022.113011</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0001-6053-6294</orcidid></addata></record> |
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subjects | adsorption biocompatible materials blood bovine serum albumin comparative study Electrokinetic measurements Fibrinogen hyaluronic acid hydrophobicity polydimethylsiloxane Protein adsorption QCM-D quartz crystal microbalance Serum albumin γ-globulin |
title | Proteins at polysaccharide-based biointerfaces: A comparative study of QCM-D and electrokinetic measurements |
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