BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states
The secondary structure and the thermostability of bovine serum albumin (BSA), before adsorption and after homomolecular displacement from silica and polystyrene particles, are studied by circular dichroism spectroscopy and differential scanning calorimetry. The structural perturbations induced by t...
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| Veröffentlicht in: | Journal of biotechnology 2000-05, Vol.79 (3), p.259-268 |
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| creator | Norde, Willem Giacomelli, Carla E |
| description | The secondary structure and the thermostability of bovine serum albumin (BSA), before adsorption and after homomolecular displacement from silica and polystyrene particles, are studied by circular dichroism spectroscopy and differential scanning calorimetry. The structural perturbations induced by the hydrophilic silica surface are reversible, i.e. BSA completely regains the native structure and stability after being exchanged. On the other hand, the adsorption on, and subsequent desorption from, polystyrene particles causes irreversible changes in the stability and (secondary) structure of BSA. The exchanged proteins have a higher denaturation temperature and a lower enthalpy of denaturation than native BSA. The α-helix content is reduced while the β-turn fraction is increased in the exchanged molecules. Both effects are more pronounced when the protein is displaced from less crowded sorbent surfaces. The irreversible surface-induced conformational change may be related to some aggregation of BSA molecules after being exposed to a hydrophobic surface. |
| doi_str_mv | 10.1016/S0168-1656(00)00242-X |
| format | Article |
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The structural perturbations induced by the hydrophilic silica surface are reversible, i.e. BSA completely regains the native structure and stability after being exchanged. On the other hand, the adsorption on, and subsequent desorption from, polystyrene particles causes irreversible changes in the stability and (secondary) structure of BSA. The exchanged proteins have a higher denaturation temperature and a lower enthalpy of denaturation than native BSA. The α-helix content is reduced while the β-turn fraction is increased in the exchanged molecules. Both effects are more pronounced when the protein is displaced from less crowded sorbent surfaces. The irreversible surface-induced conformational change may be related to some aggregation of BSA molecules after being exposed to a hydrophobic surface.</description><identifier>ISSN: 0168-1656</identifier><identifier>EISSN: 1873-4863</identifier><identifier>DOI: 10.1016/S0168-1656(00)00242-X</identifier><identifier>PMID: 10867186</identifier><identifier>CODEN: JBITD4</identifier><language>eng</language><publisher>Lausanne: Elsevier B.V</publisher><subject>Adsorption ; Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Biotechnology ; Bovine serum albumin ; Calorimetry, Differential Scanning ; Cattle ; Circular Dichroism ; Desorption ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods ; Homomolecular exchange ; Methods. Procedures. Technologies ; polystyrene ; Protein Denaturation ; Protein engineering ; Protein Renaturation ; Protein Structure, Secondary ; Proteins ; Secondary structure ; Serum Albumin, Bovine - chemistry ; Temperature ; Thermostability</subject><ispartof>Journal of biotechnology, 2000-05, Vol.79 (3), p.259-268</ispartof><rights>2000 Elsevier Science B.V.</rights><rights>2000 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-29b6c361f8d4dfdb7aadbaa95e3b03fc132d5fcb22c139e64ba81b8fe1a2a2613</citedby><cites>FETCH-LOGICAL-c473t-29b6c361f8d4dfdb7aadbaa95e3b03fc132d5fcb22c139e64ba81b8fe1a2a2613</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S016816560000242X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>309,310,314,776,780,785,786,3536,23910,23911,25119,27903,27904,65309</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1407728$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10867186$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Norde, Willem</creatorcontrib><creatorcontrib>Giacomelli, Carla E</creatorcontrib><title>BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states</title><title>Journal of biotechnology</title><addtitle>J Biotechnol</addtitle><description>The secondary structure and the thermostability of bovine serum albumin (BSA), before adsorption and after homomolecular displacement from silica and polystyrene particles, are studied by circular dichroism spectroscopy and differential scanning calorimetry. The structural perturbations induced by the hydrophilic silica surface are reversible, i.e. BSA completely regains the native structure and stability after being exchanged. On the other hand, the adsorption on, and subsequent desorption from, polystyrene particles causes irreversible changes in the stability and (secondary) structure of BSA. The exchanged proteins have a higher denaturation temperature and a lower enthalpy of denaturation than native BSA. The α-helix content is reduced while the β-turn fraction is increased in the exchanged molecules. Both effects are more pronounced when the protein is displaced from less crowded sorbent surfaces. The irreversible surface-induced conformational change may be related to some aggregation of BSA molecules after being exposed to a hydrophobic surface.</description><subject>Adsorption</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Bovine serum albumin</subject><subject>Calorimetry, Differential Scanning</subject><subject>Cattle</subject><subject>Circular Dichroism</subject><subject>Desorption</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods</subject><subject>Homomolecular exchange</subject><subject>Methods. Procedures. Technologies</subject><subject>polystyrene</subject><subject>Protein Denaturation</subject><subject>Protein engineering</subject><subject>Protein Renaturation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Secondary structure</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Temperature</subject><subject>Thermostability</subject><issn>0168-1656</issn><issn>1873-4863</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFu1DAQhi0EokvhEUA5IASHgMdObO8JlQpapEocClJv1tiedI2ySbGdUt6-2c0KuFWWxtbMN-PR_zP2Evh74KA-XM7B1KBa9Zbzd5yLRtRXj9gKjJZ1Y5R8zFZ_kSP2LOefnPNm3cJTdgTcKA1GrZj7dHlS5ZImX6aEfeU3OFxTrsKU4nBdbcbtfHryU4-porulXDkqv4mGqmyowpDH5ChUOIR9IsScx_52zuSChfJz9qTDPtOLw33Mfnz5_P30vL74dvb19OSi9o2WpRZrp7xU0JnQhC44jRgc4rol6bjsPEgR2s47IebnmlTj0IAzHQEKFArkMXuzzL1J46-JcrHbmD31PQ40TtlqENCANg-CoNuWS6FmsF1An8acE3X2JsUtpj8WuN25YPcu2J3ElnO7d8FezX2vDh9Mbkvhv65F9hl4fQAwe-y7hIOP-R_XcK3FbtGPC0azbLeRks0-0uApxES-2DDGBza5B29ppdw</recordid><startdate>20000526</startdate><enddate>20000526</enddate><creator>Norde, Willem</creator><creator>Giacomelli, Carla E</creator><general>Elsevier B.V</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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20000526</creationdate><title>BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states</title><author>Norde, Willem ; Giacomelli, Carla E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473t-29b6c361f8d4dfdb7aadbaa95e3b03fc132d5fcb22c139e64ba81b8fe1a2a2613</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adsorption</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Bovine serum albumin</topic><topic>Calorimetry, Differential Scanning</topic><topic>Cattle</topic><topic>Circular Dichroism</topic><topic>Desorption</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods</topic><topic>Homomolecular exchange</topic><topic>Methods. Procedures. Technologies</topic><topic>polystyrene</topic><topic>Protein Denaturation</topic><topic>Protein engineering</topic><topic>Protein Renaturation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Secondary structure</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Temperature</topic><topic>Thermostability</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Norde, Willem</creatorcontrib><creatorcontrib>Giacomelli, Carla E</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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Norde, Willem</au><au>Giacomelli, Carla E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states</atitle><jtitle>Journal of biotechnology</jtitle><addtitle>J Biotechnol</addtitle><date>2000-05-26</date><risdate>2000</risdate><volume>79</volume><issue>3</issue><spage>259</spage><epage>268</epage><pages>259-268</pages><issn>0168-1656</issn><eissn>1873-4863</eissn><coden>JBITD4</coden><abstract>The secondary structure and the thermostability of bovine serum albumin (BSA), before adsorption and after homomolecular displacement from silica and polystyrene particles, are studied by circular dichroism spectroscopy and differential scanning calorimetry. The structural perturbations induced by the hydrophilic silica surface are reversible, i.e. BSA completely regains the native structure and stability after being exchanged. On the other hand, the adsorption on, and subsequent desorption from, polystyrene particles causes irreversible changes in the stability and (secondary) structure of BSA. The exchanged proteins have a higher denaturation temperature and a lower enthalpy of denaturation than native BSA. The α-helix content is reduced while the β-turn fraction is increased in the exchanged molecules. Both effects are more pronounced when the protein is displaced from less crowded sorbent surfaces. The irreversible surface-induced conformational change may be related to some aggregation of BSA molecules after being exposed to a hydrophobic surface.</abstract><cop>Lausanne</cop><cop>Amsterdam</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>10867186</pmid><doi>10.1016/S0168-1656(00)00242-X</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of biotechnology, 2000-05, Vol.79 (3), p.259-268 |
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| subjects | Adsorption Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Biotechnology Bovine serum albumin Calorimetry, Differential Scanning Cattle Circular Dichroism Desorption Fundamental and applied biological sciences. Psychology General aspects, investigation methods Homomolecular exchange Methods. Procedures. Technologies polystyrene Protein Denaturation Protein engineering Protein Renaturation Protein Structure, Secondary Proteins Secondary structure Serum Albumin, Bovine - chemistry Temperature Thermostability |
| title | BSA structural changes during homomolecular exchange between the adsorbed and the dissolved states |
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