An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing
In order to obtain an ultra-sensitive molecular biosensor, we designed an auto-biotinylated bifunctional protein nanowire (bFPNw) based on the self-assembly of a yeast amyloid protein, Sup35, to which protein G and a biotin acceptor peptide (BAP) were genetically fused. These auto-biotinylated bFPNw...
Gespeichert in:
| Veröffentlicht in: | Biosensors & bioelectronics 2010-12, Vol.26 (4), p.1137-1141 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1141 |
|---|---|
| container_issue | 4 |
| container_start_page | 1137 |
| container_title | Biosensors & bioelectronics |
| container_volume | 26 |
| creator | Men, Dong Zhang, Zhi-Ping Guo, Yong-Chao Zhu, Duan-Hao Bi, Li-Jun Deng, Jiao-Yu Cui, Zong-Qiang Wei, Hong-Ping Zhang, Xian-En |
| description | In order to obtain an ultra-sensitive molecular biosensor, we designed an auto-biotinylated bifunctional protein nanowire (bFPNw) based on the self-assembly of a yeast amyloid protein, Sup35, to which protein G and a biotin acceptor peptide (BAP) were genetically fused. These auto-biotinylated bFPNws can transfer hundreds of commercially available diagnostic enzymes to an antigen–antibody complex via the biotin–avidin system, greatly enhancing the sensitivity of immune-biosensing. Compared to our previously reported seeding-induced bFPNws (
Men et al., 2009), these auto-biotinylated bFPNws gave greater signal amplification, reduced non-specific binding and improved stability. The auto-biotinylated self-assembled bFPNw molecular biosensors were applied to detect
Yersinia pestis (
Y. pestis) F1 antigen and showed a 2000- to 4000-fold increase in sensitivity compared to traditional immunoassays, demonstrating the potential use of these self-assembling protein nanowires in biosensing. |
| doi_str_mv | 10.1016/j.bios.2010.07.103 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_861534561</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0956566310004781</els_id><sourcerecordid>815965758</sourcerecordid><originalsourceid>FETCH-LOGICAL-c516t-391a68e187f8e039fc2e13a6ff08b44fc03d9acf506d47e8b3883edd9d744f033</originalsourceid><addsrcrecordid>eNqFkc2LFDEQxYMo7uzqP-BB-iLupcfKpPMFXpbFL1jwoicPIZ2uSIaeZE3Su-x_b5oZ9baeCl796vGoR8grClsKVLzbb8eQynYHTQDZNPaEbKiSrB92jD8lG9Bc9FwIdkbOS9kDgKQanpOzHWgJWrEN-XEVO7vU1DerGuLDbCtO3Rj8El0NKdq5u82pYohdtDHdh4ydT7lb5pptXzCWUMMddoc0o1tmm7s10yrHny_IM2_ngi9P84J8__jh2_Xn_ubrpy_XVze941TUnmlqhcIW3CsEpr3bIWVWeA9qHAbvgE3aOs9BTINENTKlGE6TnmTbAmMX5O3RtyX9tWCp5hCKw3m2EdNSjBKUs4EL-n-Sci245KqRl4-SVEpgA1DGG7o7oi6nUjJ6c5vDweYHQ8GsRZm9WZ9i1qIMyKatmV-f_JfxgNPfkz_NNODNCbDF2dlnG10o_zimQQPoxr0_ctg-fBcwm-ICRodTq8pVM6XwWI7fq7SyQw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1770340135</pqid></control><display><type>article</type><title>An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Men, Dong ; Zhang, Zhi-Ping ; Guo, Yong-Chao ; Zhu, Duan-Hao ; Bi, Li-Jun ; Deng, Jiao-Yu ; Cui, Zong-Qiang ; Wei, Hong-Ping ; Zhang, Xian-En</creator><creatorcontrib>Men, Dong ; Zhang, Zhi-Ping ; Guo, Yong-Chao ; Zhu, Duan-Hao ; Bi, Li-Jun ; Deng, Jiao-Yu ; Cui, Zong-Qiang ; Wei, Hong-Ping ; Zhang, Xian-En</creatorcontrib><description>In order to obtain an ultra-sensitive molecular biosensor, we designed an auto-biotinylated bifunctional protein nanowire (bFPNw) based on the self-assembly of a yeast amyloid protein, Sup35, to which protein G and a biotin acceptor peptide (BAP) were genetically fused. These auto-biotinylated bFPNws can transfer hundreds of commercially available diagnostic enzymes to an antigen–antibody complex via the biotin–avidin system, greatly enhancing the sensitivity of immune-biosensing. Compared to our previously reported seeding-induced bFPNws (
Men et al., 2009), these auto-biotinylated bFPNws gave greater signal amplification, reduced non-specific binding and improved stability. The auto-biotinylated self-assembled bFPNw molecular biosensors were applied to detect
Yersinia pestis (
Y. pestis) F1 antigen and showed a 2000- to 4000-fold increase in sensitivity compared to traditional immunoassays, demonstrating the potential use of these self-assembling protein nanowires in biosensing.</description><identifier>ISSN: 0956-5663</identifier><identifier>EISSN: 1873-4235</identifier><identifier>DOI: 10.1016/j.bios.2010.07.103</identifier><identifier>PMID: 20970983</identifier><language>eng</language><publisher>Kidlington: Elsevier B.V</publisher><subject>Amyloid ; Antigens ; Antigens, Bacterial - analysis ; Auto-biotinylated ; Awards and Prizes ; Bacterial Proteins - analysis ; Bacterial Proteins - chemistry ; Bifunctional protein nanowire ; Biological and medical sciences ; Biosensing Techniques - instrumentation ; Biosensing Techniques - methods ; Biosensing Techniques - statistics & numerical data ; Biosensors ; Biotechnology ; Biotinylation ; Cross-Linking Reagents - chemistry ; Enzymes ; Fundamental and applied biological sciences. Psychology ; Immunoassay ; Immunoassay - instrumentation ; Immunoassay - methods ; Immunoassay - statistics & numerical data ; Methods. Procedures. Technologies ; Nanocomposites ; Nanomaterials ; Nanowires ; Nanowires - chemistry ; Nanowires - ultrastructure ; Peptide Termination Factors - chemistry ; Peptide Termination Factors - ultrastructure ; Peptides ; Protein Multimerization ; Proteins ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - ultrastructure ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - ultrastructure ; Self assembly ; Ultra–sensitivity molecular biosensing ; Various methods and equipments ; Yersinia pestis ; Yersinia pestis - immunology</subject><ispartof>Biosensors & bioelectronics, 2010-12, Vol.26 (4), p.1137-1141</ispartof><rights>2010 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><rights>Copyright © 2010 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c516t-391a68e187f8e039fc2e13a6ff08b44fc03d9acf506d47e8b3883edd9d744f033</citedby><cites>FETCH-LOGICAL-c516t-391a68e187f8e039fc2e13a6ff08b44fc03d9acf506d47e8b3883edd9d744f033</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bios.2010.07.103$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>309,310,314,780,784,789,790,3550,23930,23931,25140,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23909009$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20970983$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Men, Dong</creatorcontrib><creatorcontrib>Zhang, Zhi-Ping</creatorcontrib><creatorcontrib>Guo, Yong-Chao</creatorcontrib><creatorcontrib>Zhu, Duan-Hao</creatorcontrib><creatorcontrib>Bi, Li-Jun</creatorcontrib><creatorcontrib>Deng, Jiao-Yu</creatorcontrib><creatorcontrib>Cui, Zong-Qiang</creatorcontrib><creatorcontrib>Wei, Hong-Ping</creatorcontrib><creatorcontrib>Zhang, Xian-En</creatorcontrib><title>An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing</title><title>Biosensors & bioelectronics</title><addtitle>Biosens Bioelectron</addtitle><description>In order to obtain an ultra-sensitive molecular biosensor, we designed an auto-biotinylated bifunctional protein nanowire (bFPNw) based on the self-assembly of a yeast amyloid protein, Sup35, to which protein G and a biotin acceptor peptide (BAP) were genetically fused. These auto-biotinylated bFPNws can transfer hundreds of commercially available diagnostic enzymes to an antigen–antibody complex via the biotin–avidin system, greatly enhancing the sensitivity of immune-biosensing. Compared to our previously reported seeding-induced bFPNws (
Men et al., 2009), these auto-biotinylated bFPNws gave greater signal amplification, reduced non-specific binding and improved stability. The auto-biotinylated self-assembled bFPNw molecular biosensors were applied to detect
Yersinia pestis (
Y. pestis) F1 antigen and showed a 2000- to 4000-fold increase in sensitivity compared to traditional immunoassays, demonstrating the potential use of these self-assembling protein nanowires in biosensing.</description><subject>Amyloid</subject><subject>Antigens</subject><subject>Antigens, Bacterial - analysis</subject><subject>Auto-biotinylated</subject><subject>Awards and Prizes</subject><subject>Bacterial Proteins - analysis</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bifunctional protein nanowire</subject><subject>Biological and medical sciences</subject><subject>Biosensing Techniques - instrumentation</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensing Techniques - statistics & numerical data</subject><subject>Biosensors</subject><subject>Biotechnology</subject><subject>Biotinylation</subject><subject>Cross-Linking Reagents - chemistry</subject><subject>Enzymes</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Immunoassay</subject><subject>Immunoassay - instrumentation</subject><subject>Immunoassay - methods</subject><subject>Immunoassay - statistics & numerical data</subject><subject>Methods. Procedures. Technologies</subject><subject>Nanocomposites</subject><subject>Nanomaterials</subject><subject>Nanowires</subject><subject>Nanowires - chemistry</subject><subject>Nanowires - ultrastructure</subject><subject>Peptide Termination Factors - chemistry</subject><subject>Peptide Termination Factors - ultrastructure</subject><subject>Peptides</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - ultrastructure</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - ultrastructure</subject><subject>Self assembly</subject><subject>Ultra–sensitivity molecular biosensing</subject><subject>Various methods and equipments</subject><subject>Yersinia pestis</subject><subject>Yersinia pestis - immunology</subject><issn>0956-5663</issn><issn>1873-4235</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc2LFDEQxYMo7uzqP-BB-iLupcfKpPMFXpbFL1jwoicPIZ2uSIaeZE3Su-x_b5oZ9baeCl796vGoR8grClsKVLzbb8eQynYHTQDZNPaEbKiSrB92jD8lG9Bc9FwIdkbOS9kDgKQanpOzHWgJWrEN-XEVO7vU1DerGuLDbCtO3Rj8El0NKdq5u82pYohdtDHdh4ydT7lb5pptXzCWUMMddoc0o1tmm7s10yrHny_IM2_ngi9P84J8__jh2_Xn_ubrpy_XVze941TUnmlqhcIW3CsEpr3bIWVWeA9qHAbvgE3aOs9BTINENTKlGE6TnmTbAmMX5O3RtyX9tWCp5hCKw3m2EdNSjBKUs4EL-n-Sci245KqRl4-SVEpgA1DGG7o7oi6nUjJ6c5vDweYHQ8GsRZm9WZ9i1qIMyKatmV-f_JfxgNPfkz_NNODNCbDF2dlnG10o_zimQQPoxr0_ctg-fBcwm-ICRodTq8pVM6XwWI7fq7SyQw</recordid><startdate>20101215</startdate><enddate>20101215</enddate><creator>Men, Dong</creator><creator>Zhang, Zhi-Ping</creator><creator>Guo, Yong-Chao</creator><creator>Zhu, Duan-Hao</creator><creator>Bi, Li-Jun</creator><creator>Deng, Jiao-Yu</creator><creator>Cui, Zong-Qiang</creator><creator>Wei, Hong-Ping</creator><creator>Zhang, Xian-En</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>7SP</scope><scope>7U5</scope><scope>8FD</scope><scope>L7M</scope><scope>7X8</scope><scope>7QO</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20101215</creationdate><title>An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing</title><author>Men, Dong ; Zhang, Zhi-Ping ; Guo, Yong-Chao ; Zhu, Duan-Hao ; Bi, Li-Jun ; Deng, Jiao-Yu ; Cui, Zong-Qiang ; Wei, Hong-Ping ; Zhang, Xian-En</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c516t-391a68e187f8e039fc2e13a6ff08b44fc03d9acf506d47e8b3883edd9d744f033</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amyloid</topic><topic>Antigens</topic><topic>Antigens, Bacterial - analysis</topic><topic>Auto-biotinylated</topic><topic>Awards and Prizes</topic><topic>Bacterial Proteins - analysis</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bifunctional protein nanowire</topic><topic>Biological and medical sciences</topic><topic>Biosensing Techniques - instrumentation</topic><topic>Biosensing Techniques - methods</topic><topic>Biosensing Techniques - statistics & numerical data</topic><topic>Biosensors</topic><topic>Biotechnology</topic><topic>Biotinylation</topic><topic>Cross-Linking Reagents - chemistry</topic><topic>Enzymes</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Immunoassay</topic><topic>Immunoassay - instrumentation</topic><topic>Immunoassay - methods</topic><topic>Immunoassay - statistics & numerical data</topic><topic>Methods. Procedures. Technologies</topic><topic>Nanocomposites</topic><topic>Nanomaterials</topic><topic>Nanowires</topic><topic>Nanowires - chemistry</topic><topic>Nanowires - ultrastructure</topic><topic>Peptide Termination Factors - chemistry</topic><topic>Peptide Termination Factors - ultrastructure</topic><topic>Peptides</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - ultrastructure</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - ultrastructure</topic><topic>Self assembly</topic><topic>Ultra–sensitivity molecular biosensing</topic><topic>Various methods and equipments</topic><topic>Yersinia pestis</topic><topic>Yersinia pestis - immunology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Men, Dong</creatorcontrib><creatorcontrib>Zhang, Zhi-Ping</creatorcontrib><creatorcontrib>Guo, Yong-Chao</creatorcontrib><creatorcontrib>Zhu, Duan-Hao</creatorcontrib><creatorcontrib>Bi, Li-Jun</creatorcontrib><creatorcontrib>Deng, Jiao-Yu</creatorcontrib><creatorcontrib>Cui, Zong-Qiang</creatorcontrib><creatorcontrib>Wei, Hong-Ping</creatorcontrib><creatorcontrib>Zhang, Xian-En</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>Electronics & Communications Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Technology Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Biosensors & bioelectronics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Men, Dong</au><au>Zhang, Zhi-Ping</au><au>Guo, Yong-Chao</au><au>Zhu, Duan-Hao</au><au>Bi, Li-Jun</au><au>Deng, Jiao-Yu</au><au>Cui, Zong-Qiang</au><au>Wei, Hong-Ping</au><au>Zhang, Xian-En</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing</atitle><jtitle>Biosensors & bioelectronics</jtitle><addtitle>Biosens Bioelectron</addtitle><date>2010-12-15</date><risdate>2010</risdate><volume>26</volume><issue>4</issue><spage>1137</spage><epage>1141</epage><pages>1137-1141</pages><issn>0956-5663</issn><eissn>1873-4235</eissn><abstract>In order to obtain an ultra-sensitive molecular biosensor, we designed an auto-biotinylated bifunctional protein nanowire (bFPNw) based on the self-assembly of a yeast amyloid protein, Sup35, to which protein G and a biotin acceptor peptide (BAP) were genetically fused. These auto-biotinylated bFPNws can transfer hundreds of commercially available diagnostic enzymes to an antigen–antibody complex via the biotin–avidin system, greatly enhancing the sensitivity of immune-biosensing. Compared to our previously reported seeding-induced bFPNws (
Men et al., 2009), these auto-biotinylated bFPNws gave greater signal amplification, reduced non-specific binding and improved stability. The auto-biotinylated self-assembled bFPNw molecular biosensors were applied to detect
Yersinia pestis (
Y. pestis) F1 antigen and showed a 2000- to 4000-fold increase in sensitivity compared to traditional immunoassays, demonstrating the potential use of these self-assembling protein nanowires in biosensing.</abstract><cop>Kidlington</cop><pub>Elsevier B.V</pub><pmid>20970983</pmid><doi>10.1016/j.bios.2010.07.103</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0956-5663 |
| ispartof | Biosensors & bioelectronics, 2010-12, Vol.26 (4), p.1137-1141 |
| issn | 0956-5663 1873-4235 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_861534561 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amyloid Antigens Antigens, Bacterial - analysis Auto-biotinylated Awards and Prizes Bacterial Proteins - analysis Bacterial Proteins - chemistry Bifunctional protein nanowire Biological and medical sciences Biosensing Techniques - instrumentation Biosensing Techniques - methods Biosensing Techniques - statistics & numerical data Biosensors Biotechnology Biotinylation Cross-Linking Reagents - chemistry Enzymes Fundamental and applied biological sciences. Psychology Immunoassay Immunoassay - instrumentation Immunoassay - methods Immunoassay - statistics & numerical data Methods. Procedures. Technologies Nanocomposites Nanomaterials Nanowires Nanowires - chemistry Nanowires - ultrastructure Peptide Termination Factors - chemistry Peptide Termination Factors - ultrastructure Peptides Protein Multimerization Proteins Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - ultrastructure Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - ultrastructure Self assembly Ultra–sensitivity molecular biosensing Various methods and equipments Yersinia pestis Yersinia pestis - immunology |
| title | An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T04%3A30%3A15IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=An%20auto-biotinylated%20bifunctional%20protein%20nanowire%20for%20ultra-sensitive%20molecular%20biosensing&rft.jtitle=Biosensors%20&%20bioelectronics&rft.au=Men,%20Dong&rft.date=2010-12-15&rft.volume=26&rft.issue=4&rft.spage=1137&rft.epage=1141&rft.pages=1137-1141&rft.issn=0956-5663&rft.eissn=1873-4235&rft_id=info:doi/10.1016/j.bios.2010.07.103&rft_dat=%3Cproquest_cross%3E815965758%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1770340135&rft_id=info:pmid/20970983&rft_els_id=S0956566310004781&rfr_iscdi=true |