Protein–surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)
The aim of this work was to study the dynamics of proteins near solid surfaces in the presence or absence of competing surfactants by means of total internal reflection fluorescence correlation spectroscopy (TIR-FCS). Two different proteins were studied, bovine serum albumin (BSA) and Thermomyces la...
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| Veröffentlicht in: | Journal of colloid and interface science 2008, Vol.317 (2), p.449-457 |
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| creator | Sonesson, Andreas W. Blom, Hans Hassler, Kai Elofsson, Ulla M. Callisen, Thomas H. Widengren, Jerker Brismar, Hjalmar |
| description | The aim of this work was to study the dynamics of proteins near solid surfaces in the presence or absence of competing surfactants by means of total internal reflection fluorescence correlation spectroscopy (TIR-FCS). Two different proteins were studied, bovine serum albumin (BSA) and
Thermomyces lanuginosus lipase (TLL). A nonionic/anionic (C
12E
6/LAS) surfactant composition was used to mimic a detergent formulation and the surfaces used were C18 terminated glass. It was found that with increasing surfactant concentrations the term in the autocorrelation function (ACF) representing surface binding decreased. This suggested that the proteins were competed off the hydrophobic surface by the surfactant. When fitting the measured ACF to a model for surface kinetics, it was seen that with raised C
12E
6/LAS concentration, the surface interaction rate increased for both proteins. Under these experimental conditions this meant that the time the protein was bound to the surface decreased. At 10 μM C
12E
6/LAS the surface interaction was not visible for BSA, whereas it was still distinguishable in the ACF for TLL. This indicated that TLL had a higher affinity than BSA for the C18 surface. The study showed that TIR-FCS provides a useful tool to quantify the surfactant effect on proteins adsorption. |
| doi_str_mv | 10.1016/j.jcis.2007.09.089 |
| format | Article |
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Thermomyces lanuginosus lipase (TLL). A nonionic/anionic (C
12E
6/LAS) surfactant composition was used to mimic a detergent formulation and the surfaces used were C18 terminated glass. It was found that with increasing surfactant concentrations the term in the autocorrelation function (ACF) representing surface binding decreased. This suggested that the proteins were competed off the hydrophobic surface by the surfactant. When fitting the measured ACF to a model for surface kinetics, it was seen that with raised C
12E
6/LAS concentration, the surface interaction rate increased for both proteins. Under these experimental conditions this meant that the time the protein was bound to the surface decreased. At 10 μM C
12E
6/LAS the surface interaction was not visible for BSA, whereas it was still distinguishable in the ACF for TLL. This indicated that TLL had a higher affinity than BSA for the C18 surface. The study showed that TIR-FCS provides a useful tool to quantify the surfactant effect on proteins adsorption.</description><identifier>ISSN: 0021-9797</identifier><identifier>ISSN: 1095-7103</identifier><identifier>EISSN: 1095-7103</identifier><identifier>DOI: 10.1016/j.jcis.2007.09.089</identifier><identifier>PMID: 17950302</identifier><identifier>CODEN: JCISA5</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Animals ; Ascomycota - enzymology ; Binding Sites ; BSA ; C 12E 6/LAS ; Cattle ; Chemistry ; Colloidal state and disperse state ; Exact sciences and technology ; Fluorescent Dyes ; Fysik ; General and physical chemistry ; Hydrophobic and Hydrophilic Interactions ; Hydrophobic surface ; Lasers ; Lipase ; Lipase - chemistry ; Medicin och hälsovetenskap ; NATURAL SCIENCES ; NATURVETENSKAP ; Physics ; Proteins - chemistry ; Protein–surfactant interactions ; Serum Albumin, Bovine - chemistry ; Spectrometry, Fluorescence - methods ; Surface physical chemistry ; Surface Properties ; Surface-Active Agents - chemistry ; TIR-FCS</subject><ispartof>Journal of colloid and interface science, 2008, Vol.317 (2), p.449-457</ispartof><rights>2007 Elsevier Inc.</rights><rights>2008 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c544t-f2d662ed2f2e9bdc51cf8feccf3996491a8dbad53c2e29c4a74a0a6f71e84b953</citedby><cites>FETCH-LOGICAL-c544t-f2d662ed2f2e9bdc51cf8feccf3996491a8dbad53c2e29c4a74a0a6f71e84b953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jcis.2007.09.089$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19912922$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17950302$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-6931$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:ri:diva-26663$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:116298256$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Sonesson, Andreas W.</creatorcontrib><creatorcontrib>Blom, Hans</creatorcontrib><creatorcontrib>Hassler, Kai</creatorcontrib><creatorcontrib>Elofsson, Ulla M.</creatorcontrib><creatorcontrib>Callisen, Thomas H.</creatorcontrib><creatorcontrib>Widengren, Jerker</creatorcontrib><creatorcontrib>Brismar, Hjalmar</creatorcontrib><title>Protein–surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)</title><title>Journal of colloid and interface science</title><addtitle>J Colloid Interface Sci</addtitle><description>The aim of this work was to study the dynamics of proteins near solid surfaces in the presence or absence of competing surfactants by means of total internal reflection fluorescence correlation spectroscopy (TIR-FCS). Two different proteins were studied, bovine serum albumin (BSA) and
Thermomyces lanuginosus lipase (TLL). A nonionic/anionic (C
12E
6/LAS) surfactant composition was used to mimic a detergent formulation and the surfaces used were C18 terminated glass. It was found that with increasing surfactant concentrations the term in the autocorrelation function (ACF) representing surface binding decreased. This suggested that the proteins were competed off the hydrophobic surface by the surfactant. When fitting the measured ACF to a model for surface kinetics, it was seen that with raised C
12E
6/LAS concentration, the surface interaction rate increased for both proteins. Under these experimental conditions this meant that the time the protein was bound to the surface decreased. At 10 μM C
12E
6/LAS the surface interaction was not visible for BSA, whereas it was still distinguishable in the ACF for TLL. This indicated that TLL had a higher affinity than BSA for the C18 surface. The study showed that TIR-FCS provides a useful tool to quantify the surfactant effect on proteins adsorption.</description><subject>Animals</subject><subject>Ascomycota - enzymology</subject><subject>Binding Sites</subject><subject>BSA</subject><subject>C 12E 6/LAS</subject><subject>Cattle</subject><subject>Chemistry</subject><subject>Colloidal state and disperse state</subject><subject>Exact sciences and technology</subject><subject>Fluorescent Dyes</subject><subject>Fysik</subject><subject>General and physical chemistry</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobic surface</subject><subject>Lasers</subject><subject>Lipase</subject><subject>Lipase - chemistry</subject><subject>Medicin och hälsovetenskap</subject><subject>NATURAL SCIENCES</subject><subject>NATURVETENSKAP</subject><subject>Physics</subject><subject>Proteins - chemistry</subject><subject>Protein–surfactant interactions</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Spectrometry, Fluorescence - methods</subject><subject>Surface physical chemistry</subject><subject>Surface Properties</subject><subject>Surface-Active Agents - chemistry</subject><subject>TIR-FCS</subject><issn>0021-9797</issn><issn>1095-7103</issn><issn>1095-7103</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNksFu1DAQhiMEokvhBTigXEAglGA7iRNLXKqFQqVKIChcLcces95m49R2qPbGM8Ab8iQ4TWhPRZw88nz_79H4T5LHGOUYYfpqm2-l8TlBqM4Ry1HD7iQrjFiV1RgVd5MVQgRnrGb1QfLA-y1CGFcVu58c4JpVqEBklfz86GwA0__-8cuPTgsZRB9S0wdwsTa296kI6WavnB02tjVy7kUQfOrDqAyo9NKETRpsEN3c7WPhQHdw5ZDqbrQOvIReQiqtc9CJq4YfIuGsl3bYp8_PTj5lx-vPLx4m97ToPDxazsPky_Hbs_X77PTDu5P10Wkmq7IMmSaKUgKKaAKsVbLCUjcapNQFY7RkWDSqFaoqJAHCZCnqUiBBdY2hKVtWFYdJNvv6SxjGlg_O7ITbcysMX67OYwW8ojWlReTZrfzgrLoR_RViTAlrSEWj9uWt2jfm6xG37ht3hhM6v_Qf9HnYcMoKHOlnMx2HuBjBB74zcdldJ3qwo-c1immpWRlBMoMy7tzHD7o2xohPieJbPiWKT4niiPGYqCh6sriP7Q7UjWSJUASeLoDwUnTaiX7yuOYYw4SRiXs9cxD_9LsBx700UySUcTEGXFnzrzn-AE7t8fY</recordid><startdate>2008</startdate><enddate>2008</enddate><creator>Sonesson, Andreas W.</creator><creator>Blom, Hans</creator><creator>Hassler, Kai</creator><creator>Elofsson, Ulla M.</creator><creator>Callisen, Thomas H.</creator><creator>Widengren, Jerker</creator><creator>Brismar, Hjalmar</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8V</scope></search><sort><creationdate>2008</creationdate><title>Protein–surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)</title><author>Sonesson, Andreas W. ; Blom, Hans ; Hassler, Kai ; Elofsson, Ulla M. ; Callisen, Thomas H. ; Widengren, Jerker ; Brismar, Hjalmar</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c544t-f2d662ed2f2e9bdc51cf8feccf3996491a8dbad53c2e29c4a74a0a6f71e84b953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Ascomycota - enzymology</topic><topic>Binding Sites</topic><topic>BSA</topic><topic>C 12E 6/LAS</topic><topic>Cattle</topic><topic>Chemistry</topic><topic>Colloidal state and disperse state</topic><topic>Exact sciences and technology</topic><topic>Fluorescent Dyes</topic><topic>Fysik</topic><topic>General and physical chemistry</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hydrophobic surface</topic><topic>Lasers</topic><topic>Lipase</topic><topic>Lipase - chemistry</topic><topic>Medicin och hälsovetenskap</topic><topic>NATURAL SCIENCES</topic><topic>NATURVETENSKAP</topic><topic>Physics</topic><topic>Proteins - chemistry</topic><topic>Protein–surfactant interactions</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Spectrometry, Fluorescence - methods</topic><topic>Surface physical chemistry</topic><topic>Surface Properties</topic><topic>Surface-Active Agents - chemistry</topic><topic>TIR-FCS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sonesson, Andreas W.</creatorcontrib><creatorcontrib>Blom, Hans</creatorcontrib><creatorcontrib>Hassler, Kai</creatorcontrib><creatorcontrib>Elofsson, Ulla M.</creatorcontrib><creatorcontrib>Callisen, Thomas H.</creatorcontrib><creatorcontrib>Widengren, Jerker</creatorcontrib><creatorcontrib>Brismar, Hjalmar</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Kungliga Tekniska Högskolan</collection><jtitle>Journal of colloid and interface science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sonesson, Andreas W.</au><au>Blom, Hans</au><au>Hassler, Kai</au><au>Elofsson, Ulla M.</au><au>Callisen, Thomas H.</au><au>Widengren, Jerker</au><au>Brismar, Hjalmar</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein–surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS)</atitle><jtitle>Journal of colloid and interface science</jtitle><addtitle>J Colloid Interface Sci</addtitle><date>2008</date><risdate>2008</risdate><volume>317</volume><issue>2</issue><spage>449</spage><epage>457</epage><pages>449-457</pages><issn>0021-9797</issn><issn>1095-7103</issn><eissn>1095-7103</eissn><coden>JCISA5</coden><abstract>The aim of this work was to study the dynamics of proteins near solid surfaces in the presence or absence of competing surfactants by means of total internal reflection fluorescence correlation spectroscopy (TIR-FCS). Two different proteins were studied, bovine serum albumin (BSA) and
Thermomyces lanuginosus lipase (TLL). A nonionic/anionic (C
12E
6/LAS) surfactant composition was used to mimic a detergent formulation and the surfaces used were C18 terminated glass. It was found that with increasing surfactant concentrations the term in the autocorrelation function (ACF) representing surface binding decreased. This suggested that the proteins were competed off the hydrophobic surface by the surfactant. When fitting the measured ACF to a model for surface kinetics, it was seen that with raised C
12E
6/LAS concentration, the surface interaction rate increased for both proteins. Under these experimental conditions this meant that the time the protein was bound to the surface decreased. At 10 μM C
12E
6/LAS the surface interaction was not visible for BSA, whereas it was still distinguishable in the ACF for TLL. This indicated that TLL had a higher affinity than BSA for the C18 surface. The study showed that TIR-FCS provides a useful tool to quantify the surfactant effect on proteins adsorption.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>17950302</pmid><doi>10.1016/j.jcis.2007.09.089</doi><tpages>9</tpages></addata></record> |
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| subjects | Animals Ascomycota - enzymology Binding Sites BSA C 12E 6/LAS Cattle Chemistry Colloidal state and disperse state Exact sciences and technology Fluorescent Dyes Fysik General and physical chemistry Hydrophobic and Hydrophilic Interactions Hydrophobic surface Lasers Lipase Lipase - chemistry Medicin och hälsovetenskap NATURAL SCIENCES NATURVETENSKAP Physics Proteins - chemistry Protein–surfactant interactions Serum Albumin, Bovine - chemistry Spectrometry, Fluorescence - methods Surface physical chemistry Surface Properties Surface-Active Agents - chemistry TIR-FCS |
| title | Protein–surfactant interactions at hydrophobic interfaces studied with total internal reflection fluorescence correlation spectroscopy (TIR-FCS) |
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