A Stereocomplex Platform Efficiently Detecting Antigen−Antibody Interactions
Ultrathin poly(methyl methacrylate) (PMMA) stereocomplex films with macromolecularly double-stranded regular nanostructures were prepared by layer-by-layer assembly of isotactic and syndiotactic PMMAs on solid surfaces. Antibodies were immobilized through the Fc region-capturing protein A, which had...
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| Veröffentlicht in: | Bioconjugate chemistry 2007-03, Vol.18 (2), p.355-362 |
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| container_title | Bioconjugate chemistry |
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| creator | Serizawa, Takeshi Nagasaka, Yuya Matsuno, Hisao Shimoyama, Masakazu Kurita, Kimio |
| description | Ultrathin poly(methyl methacrylate) (PMMA) stereocomplex films with macromolecularly double-stranded regular nanostructures were prepared by layer-by-layer assembly of isotactic and syndiotactic PMMAs on solid surfaces. Antibodies were immobilized through the Fc region-capturing protein A, which had been physically adsorbed on the complex film, and the binding of antigens to immobilized antibodies was quantitatively investigated by the quartz crystal microbalance technique. Greater amounts of protein A with native forms were adsorbed on the complex film than those on conventional single-component PMMA films. Antibodies with high target-binding activities were also immobilized on the complex film. A greater amount of antigens could be detected on the complex film. The activity of protein A was maintained on the complex for a long time even within a dried state. The mechanism for the preservation of protein native forms on the complex surface was speculated by analyzing the physical adsorption of proteins with various secondary structures. Stereocomplex films can be utilized as novel coating nanomaterials for efficiently detecting protein−protein interactions. |
| doi_str_mv | 10.1021/bc060225k |
| format | Article |
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Antibodies were immobilized through the Fc region-capturing protein A, which had been physically adsorbed on the complex film, and the binding of antigens to immobilized antibodies was quantitatively investigated by the quartz crystal microbalance technique. Greater amounts of protein A with native forms were adsorbed on the complex film than those on conventional single-component PMMA films. Antibodies with high target-binding activities were also immobilized on the complex film. A greater amount of antigens could be detected on the complex film. The activity of protein A was maintained on the complex for a long time even within a dried state. The mechanism for the preservation of protein native forms on the complex surface was speculated by analyzing the physical adsorption of proteins with various secondary structures. Stereocomplex films can be utilized as novel coating nanomaterials for efficiently detecting protein−protein interactions.</description><identifier>ISSN: 1043-1802</identifier><identifier>EISSN: 1520-4812</identifier><identifier>DOI: 10.1021/bc060225k</identifier><identifier>PMID: 17298028</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Antigen-Antibody Reactions ; Antigens ; Binding sites ; Biochemistry ; Biocompatible Materials ; Biofilms ; Biosensing Techniques ; Cattle ; Electrochemistry ; Humans ; Immunoglobulin G - immunology ; Immunoglobulin G - metabolism ; Immunoglobulins ; Microscopy, Atomic Force ; Molecular structure ; Nanoparticles ; Nanostructures ; Polymethyl Methacrylate - chemistry ; Proteins ; Proteins - chemistry ; Proteins - immunology ; Proteins - metabolism ; Quartz - chemistry ; Serum Albumin - chemistry ; Serum Albumin - immunology ; Serum Albumin - metabolism ; Serum Albumin, Bovine - chemistry ; Serum Albumin, Bovine - immunology ; Serum Albumin, Bovine - metabolism ; Staphylococcal Protein A - immunology ; Staphylococcal Protein A - metabolism ; Surface Properties</subject><ispartof>Bioconjugate chemistry, 2007-03, Vol.18 (2), p.355-362</ispartof><rights>Copyright © 2007 American Chemical Society</rights><rights>Copyright American Chemical Society Mar 2007</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a475t-ac757d6aad18ab7c6f52e2df443a1960c16c0d211b28dd3be6563f2189f00a23</citedby><cites>FETCH-LOGICAL-a475t-ac757d6aad18ab7c6f52e2df443a1960c16c0d211b28dd3be6563f2189f00a23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bc060225k$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bc060225k$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17298028$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serizawa, Takeshi</creatorcontrib><creatorcontrib>Nagasaka, Yuya</creatorcontrib><creatorcontrib>Matsuno, Hisao</creatorcontrib><creatorcontrib>Shimoyama, Masakazu</creatorcontrib><creatorcontrib>Kurita, Kimio</creatorcontrib><title>A Stereocomplex Platform Efficiently Detecting Antigen−Antibody Interactions</title><title>Bioconjugate chemistry</title><addtitle>Bioconjugate Chem</addtitle><description>Ultrathin poly(methyl methacrylate) (PMMA) stereocomplex films with macromolecularly double-stranded regular nanostructures were prepared by layer-by-layer assembly of isotactic and syndiotactic PMMAs on solid surfaces. Antibodies were immobilized through the Fc region-capturing protein A, which had been physically adsorbed on the complex film, and the binding of antigens to immobilized antibodies was quantitatively investigated by the quartz crystal microbalance technique. Greater amounts of protein A with native forms were adsorbed on the complex film than those on conventional single-component PMMA films. Antibodies with high target-binding activities were also immobilized on the complex film. A greater amount of antigens could be detected on the complex film. The activity of protein A was maintained on the complex for a long time even within a dried state. The mechanism for the preservation of protein native forms on the complex surface was speculated by analyzing the physical adsorption of proteins with various secondary structures. Stereocomplex films can be utilized as novel coating nanomaterials for efficiently detecting protein−protein interactions.</description><subject>Animals</subject><subject>Antigen-Antibody Reactions</subject><subject>Antigens</subject><subject>Binding sites</subject><subject>Biochemistry</subject><subject>Biocompatible Materials</subject><subject>Biofilms</subject><subject>Biosensing Techniques</subject><subject>Cattle</subject><subject>Electrochemistry</subject><subject>Humans</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin G - metabolism</subject><subject>Immunoglobulins</subject><subject>Microscopy, Atomic Force</subject><subject>Molecular structure</subject><subject>Nanoparticles</subject><subject>Nanostructures</subject><subject>Polymethyl Methacrylate - chemistry</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteins - immunology</subject><subject>Proteins - metabolism</subject><subject>Quartz - chemistry</subject><subject>Serum Albumin - chemistry</subject><subject>Serum Albumin - immunology</subject><subject>Serum Albumin - metabolism</subject><subject>Serum Albumin, Bovine - chemistry</subject><subject>Serum Albumin, Bovine - immunology</subject><subject>Serum Albumin, Bovine - metabolism</subject><subject>Staphylococcal Protein A - immunology</subject><subject>Staphylococcal Protein A - metabolism</subject><subject>Surface Properties</subject><issn>1043-1802</issn><issn>1520-4812</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0c1O3DAQB3CralUo7aEvUEWVWqmH0PE4tpPjigWKgBaJPfRmOY6NAkm82F6JfYOeeUSeBKNdgdQeevLI89PfH0PIRwr7FJB-bw0IQOQ3r8gu5QhlVVN8nWuoWElrwB3yLsZrAGhojW_JDpXY5O16l_ycFZfJBuuNH5eDvSsuBp2cD2Nx6FxvejulYV3MbbIm9dNVMZtSf2Wnhz_3T1Xru3VxMuUAndt-iu_JG6eHaD9s1z2yODpcHPwoz34dnxzMzkpdSZ5KbSSXndC6o7VupRGOo8XOVRXTtBFgqDDQIaUt1l3HWiu4YA5p3TgAjWyPfN3ELoO_XdmY1NhHY4dBT9avopLAQDLO_gsRKkQGTYaf_4LXfhWm_AaFVGQmBc_o2waZ4GMM1qll6Ecd1oqCepqEep5Etp-2gat2tN2L3H59BuUG9DHZu-e-DjdKSCa5WlxcqmN5Om9-z0_VefZfNl6b-HK5fw9-BCkQnqs</recordid><startdate>20070301</startdate><enddate>20070301</enddate><creator>Serizawa, Takeshi</creator><creator>Nagasaka, Yuya</creator><creator>Matsuno, Hisao</creator><creator>Shimoyama, Masakazu</creator><creator>Kurita, Kimio</creator><general>American Chemical Society</general><scope>BSCLL</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>7TM</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20070301</creationdate><title>A Stereocomplex Platform Efficiently Detecting Antigen−Antibody Interactions</title><author>Serizawa, Takeshi ; Nagasaka, Yuya ; Matsuno, Hisao ; Shimoyama, Masakazu ; Kurita, Kimio</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a475t-ac757d6aad18ab7c6f52e2df443a1960c16c0d211b28dd3be6563f2189f00a23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Animals</topic><topic>Antigen-Antibody Reactions</topic><topic>Antigens</topic><topic>Binding sites</topic><topic>Biochemistry</topic><topic>Biocompatible Materials</topic><topic>Biofilms</topic><topic>Biosensing Techniques</topic><topic>Cattle</topic><topic>Electrochemistry</topic><topic>Humans</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin G - metabolism</topic><topic>Immunoglobulins</topic><topic>Microscopy, Atomic Force</topic><topic>Molecular structure</topic><topic>Nanoparticles</topic><topic>Nanostructures</topic><topic>Polymethyl Methacrylate - chemistry</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Proteins - immunology</topic><topic>Proteins - metabolism</topic><topic>Quartz - chemistry</topic><topic>Serum Albumin - chemistry</topic><topic>Serum Albumin - immunology</topic><topic>Serum Albumin - metabolism</topic><topic>Serum Albumin, Bovine - chemistry</topic><topic>Serum Albumin, Bovine - immunology</topic><topic>Serum Albumin, Bovine - metabolism</topic><topic>Staphylococcal Protein A - immunology</topic><topic>Staphylococcal Protein A - metabolism</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serizawa, Takeshi</creatorcontrib><creatorcontrib>Nagasaka, Yuya</creatorcontrib><creatorcontrib>Matsuno, Hisao</creatorcontrib><creatorcontrib>Shimoyama, Masakazu</creatorcontrib><creatorcontrib>Kurita, Kimio</creatorcontrib><collection>Istex</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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioconjugate chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Serizawa, Takeshi</au><au>Nagasaka, Yuya</au><au>Matsuno, Hisao</au><au>Shimoyama, Masakazu</au><au>Kurita, Kimio</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Stereocomplex Platform Efficiently Detecting Antigen−Antibody Interactions</atitle><jtitle>Bioconjugate chemistry</jtitle><addtitle>Bioconjugate Chem</addtitle><date>2007-03-01</date><risdate>2007</risdate><volume>18</volume><issue>2</issue><spage>355</spage><epage>362</epage><pages>355-362</pages><issn>1043-1802</issn><eissn>1520-4812</eissn><abstract>Ultrathin poly(methyl methacrylate) (PMMA) stereocomplex films with macromolecularly double-stranded regular nanostructures were prepared by layer-by-layer assembly of isotactic and syndiotactic PMMAs on solid surfaces. Antibodies were immobilized through the Fc region-capturing protein A, which had been physically adsorbed on the complex film, and the binding of antigens to immobilized antibodies was quantitatively investigated by the quartz crystal microbalance technique. Greater amounts of protein A with native forms were adsorbed on the complex film than those on conventional single-component PMMA films. Antibodies with high target-binding activities were also immobilized on the complex film. A greater amount of antigens could be detected on the complex film. The activity of protein A was maintained on the complex for a long time even within a dried state. The mechanism for the preservation of protein native forms on the complex surface was speculated by analyzing the physical adsorption of proteins with various secondary structures. Stereocomplex films can be utilized as novel coating nanomaterials for efficiently detecting protein−protein interactions.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>17298028</pmid><doi>10.1021/bc060225k</doi><tpages>8</tpages></addata></record> |
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| ispartof | Bioconjugate chemistry, 2007-03, Vol.18 (2), p.355-362 |
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| source | ACS Publications; MEDLINE |
| subjects | Animals Antigen-Antibody Reactions Antigens Binding sites Biochemistry Biocompatible Materials Biofilms Biosensing Techniques Cattle Electrochemistry Humans Immunoglobulin G - immunology Immunoglobulin G - metabolism Immunoglobulins Microscopy, Atomic Force Molecular structure Nanoparticles Nanostructures Polymethyl Methacrylate - chemistry Proteins Proteins - chemistry Proteins - immunology Proteins - metabolism Quartz - chemistry Serum Albumin - chemistry Serum Albumin - immunology Serum Albumin - metabolism Serum Albumin, Bovine - chemistry Serum Albumin, Bovine - immunology Serum Albumin, Bovine - metabolism Staphylococcal Protein A - immunology Staphylococcal Protein A - metabolism Surface Properties |
| title | A Stereocomplex Platform Efficiently Detecting Antigen−Antibody Interactions |
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