Detection of Protein Orientation on the Silica Microsphere Surface Using Transverse Electric/Transverse Magnetic Whispering Gallery Modes
The state of adsorbed protein molecules can be examined by comparing the shifts in a narrow line resonance wavelength of transverse electric (TE) and transverse magnetic (TM) whispering gallery modes (WGM) when the molecules adsorb onto a transparent microsphere that houses WGM. In adsorption of bov...
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| Veröffentlicht in: | Biophysical journal 2007-06, Vol.92 (12), p.4466-4472 |
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| creator | Noto, Mayumi Keng, David Teraoka, Iwao Arnold, Stephen |
| description | The state of adsorbed protein molecules can be examined by comparing the shifts in a narrow line resonance wavelength of transverse electric (TE) and transverse magnetic (TM) whispering gallery modes (WGM) when the molecules adsorb onto a transparent microsphere that houses WGM. In adsorption of bovine serum albumin (BSA) onto an aminopropyl-modified silica microsphere, the TM/TE shift ratio indicated highly anisotropic polarizability of BSA in the direction normal to the surface, most likely ascribed to anchoring the heart-shaped protein molecule by one of its tips. The polarization-dependent resonance shift was confirmed when the surrounding refractive index was uniformly changed by adding salt, which would simulate adsorption of large objects. |
| doi_str_mv | 10.1529/biophysj.106.103200 |
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In adsorption of bovine serum albumin (BSA) onto an aminopropyl-modified silica microsphere, the TM/TE shift ratio indicated highly anisotropic polarizability of BSA in the direction normal to the surface, most likely ascribed to anchoring the heart-shaped protein molecule by one of its tips. The polarization-dependent resonance shift was confirmed when the surrounding refractive index was uniformly changed by adding salt, which would simulate adsorption of large objects.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1529/biophysj.106.103200</identifier><identifier>PMID: 17400701</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adsorption ; Biophysics ; Coated Materials, Biocompatible - chemistry ; Electromagnetic Fields ; Magnetics ; Materials Testing - methods ; Microspheres ; NMR ; Nuclear magnetic resonance ; Protein Binding ; Protein Conformation ; Proteins ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - ultrastructure ; Silica ; Silicon Dioxide - chemistry ; Spectroscopy, Imaging, Other Techniques ; Surface Properties</subject><ispartof>Biophysical journal, 2007-06, Vol.92 (12), p.4466-4472</ispartof><rights>2007 The Biophysical Society</rights><rights>Copyright Biophysical Society Jun 15, 2007</rights><rights>Copyright © 2007, Biophysical Society 2007</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c550t-eb9a5697a334fbe85f043775dee4777ac8681537b6a7ab073b60ebaf3bf294e03</citedby><cites>FETCH-LOGICAL-c550t-eb9a5697a334fbe85f043775dee4777ac8681537b6a7ab073b60ebaf3bf294e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1877779/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1529/biophysj.106.103200$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,3550,27924,27925,45995,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17400701$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Noto, Mayumi</creatorcontrib><creatorcontrib>Keng, David</creatorcontrib><creatorcontrib>Teraoka, Iwao</creatorcontrib><creatorcontrib>Arnold, Stephen</creatorcontrib><title>Detection of Protein Orientation on the Silica Microsphere Surface Using Transverse Electric/Transverse Magnetic Whispering Gallery Modes</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>The state of adsorbed protein molecules can be examined by comparing the shifts in a narrow line resonance wavelength of transverse electric (TE) and transverse magnetic (TM) whispering gallery modes (WGM) when the molecules adsorb onto a transparent microsphere that houses WGM. In adsorption of bovine serum albumin (BSA) onto an aminopropyl-modified silica microsphere, the TM/TE shift ratio indicated highly anisotropic polarizability of BSA in the direction normal to the surface, most likely ascribed to anchoring the heart-shaped protein molecule by one of its tips. The polarization-dependent resonance shift was confirmed when the surrounding refractive index was uniformly changed by adding salt, which would simulate adsorption of large objects.</description><subject>Adsorption</subject><subject>Biophysics</subject><subject>Coated Materials, Biocompatible - chemistry</subject><subject>Electromagnetic Fields</subject><subject>Magnetics</subject><subject>Materials Testing - methods</subject><subject>Microspheres</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - ultrastructure</subject><subject>Silica</subject><subject>Silicon Dioxide - chemistry</subject><subject>Spectroscopy, Imaging, Other Techniques</subject><subject>Surface Properties</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNp9UcFu1DAUtBCILoUvQEIWB25pn5M4Tg4godIWpK6KRCuOluO8bLzK2sFOVtpP4K_rKAsUDhwsS-OZeZ43hLxmcMZ4Wp3Xxg3dIWzPGBTxZCnAE7JiPE8TgLJ4SlYAUCRZXvET8iKELQBLObDn5ISJHEAAW5Gfn3BEPRpnqWvpV-9GNJbeeoN2VAts6dgh_WZ6oxVdG-1dGDr0EZp8qzTS-2Dsht55ZcMefUB62UdLb_T5I2ytNhZHo-n3zoQB_Sy5Vn2P_kDXrsHwkjxrVR_w1fE-JfdXl3cXn5Ob2-svFx9vEs05jAnWleJFJVSW5W2NJW8hz4TgDWIuhFC6LErGM1EXSqgaRFYXgLVqs7pNqxwhOyUfFt9hqnfY6BjUq14O3uyUP0injPz7xZpObtxesjL6iyoavDsaePdjwjDKnQka-15ZdFOQAnheVWKe9PYf4tZN3sZwMmVcQMFgdssW0rzX4LH9_RMGcu5Z_uo5AoVceo6qN49D_NEci42E9wsB4yr3Br0MOnaqsTE-liMbZ_474AFRqL7h</recordid><startdate>20070615</startdate><enddate>20070615</enddate><creator>Noto, Mayumi</creator><creator>Keng, David</creator><creator>Teraoka, Iwao</creator><creator>Arnold, Stephen</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20070615</creationdate><title>Detection of Protein Orientation on the Silica Microsphere Surface Using Transverse Electric/Transverse Magnetic Whispering Gallery Modes</title><author>Noto, Mayumi ; Keng, David ; Teraoka, Iwao ; Arnold, Stephen</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c550t-eb9a5697a334fbe85f043775dee4777ac8681537b6a7ab073b60ebaf3bf294e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Adsorption</topic><topic>Biophysics</topic><topic>Coated Materials, Biocompatible - chemistry</topic><topic>Electromagnetic Fields</topic><topic>Magnetics</topic><topic>Materials Testing - methods</topic><topic>Microspheres</topic><topic>NMR</topic><topic>Nuclear magnetic resonance</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Proteins</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - ultrastructure</topic><topic>Silica</topic><topic>Silicon Dioxide - chemistry</topic><topic>Spectroscopy, Imaging, Other Techniques</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noto, Mayumi</creatorcontrib><creatorcontrib>Keng, David</creatorcontrib><creatorcontrib>Teraoka, Iwao</creatorcontrib><creatorcontrib>Arnold, Stephen</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Noto, Mayumi</au><au>Keng, David</au><au>Teraoka, Iwao</au><au>Arnold, Stephen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of Protein Orientation on the Silica Microsphere Surface Using Transverse Electric/Transverse Magnetic Whispering Gallery Modes</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2007-06-15</date><risdate>2007</risdate><volume>92</volume><issue>12</issue><spage>4466</spage><epage>4472</epage><pages>4466-4472</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>The state of adsorbed protein molecules can be examined by comparing the shifts in a narrow line resonance wavelength of transverse electric (TE) and transverse magnetic (TM) whispering gallery modes (WGM) when the molecules adsorb onto a transparent microsphere that houses WGM. In adsorption of bovine serum albumin (BSA) onto an aminopropyl-modified silica microsphere, the TM/TE shift ratio indicated highly anisotropic polarizability of BSA in the direction normal to the surface, most likely ascribed to anchoring the heart-shaped protein molecule by one of its tips. The polarization-dependent resonance shift was confirmed when the surrounding refractive index was uniformly changed by adding salt, which would simulate adsorption of large objects.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17400701</pmid><doi>10.1529/biophysj.106.103200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 2007-06, Vol.92 (12), p.4466-4472 |
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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adsorption Biophysics Coated Materials, Biocompatible - chemistry Electromagnetic Fields Magnetics Materials Testing - methods Microspheres NMR Nuclear magnetic resonance Protein Binding Protein Conformation Proteins Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - ultrastructure Silica Silicon Dioxide - chemistry Spectroscopy, Imaging, Other Techniques Surface Properties |
| title | Detection of Protein Orientation on the Silica Microsphere Surface Using Transverse Electric/Transverse Magnetic Whispering Gallery Modes |
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