Therapeutic antibodies: Discovery and development using the ProteOn XPR36 biosensor interaction array system
Therapeutic monoclonal antibodies are becoming a significant and rapidly growing class of therapeutic pharmaceuticals. Their discovery and development requires fast and high-throughput methodologies for screening and selecting appropriate candidate antibodies having high affinity for the target as w...
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| Veröffentlicht in: | Analytical biochemistry 2010-11, Vol.406 (2), p.147-156 |
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| container_title | Analytical biochemistry |
| container_volume | 406 |
| creator | Bronner, Vered Denkberg, Galit Peled, Mira Elbaz, Yael Zahavi, Efrat Kasoto, Harel Reiter, Yoram Notcovich, Ariel Bravman, Tsafrir |
| description | Therapeutic monoclonal antibodies are becoming a significant and rapidly growing class of therapeutic pharmaceuticals. Their discovery and development requires fast and high-throughput methodologies for screening and selecting appropriate candidate antibodies having high affinity for the target as well as high specificity and low cross-reactivity. This study demonstrates the use of the ProteOn XPR36 protein interaction array system and its novel approach, termed One-Shot Kinetics, for the rapid screening and selection of high-affinity antibodies. This approach allows multiple quantitative protein binding analyses in parallel, providing association, dissociation, and affinity constants for several antibodies or supernatants simultaneously in one experiment. We show that the ProteOn XPR36 system is a valuable tool for use across multiple stages of the therapeutic antibody discovery and development process, enabling efficient and rapid screening after panning, affinity maturation, assay validation, and clone selection. |
| doi_str_mv | 10.1016/j.ab.2010.07.005 |
| format | Article |
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Their discovery and development requires fast and high-throughput methodologies for screening and selecting appropriate candidate antibodies having high affinity for the target as well as high specificity and low cross-reactivity. This study demonstrates the use of the ProteOn XPR36 protein interaction array system and its novel approach, termed One-Shot Kinetics, for the rapid screening and selection of high-affinity antibodies. This approach allows multiple quantitative protein binding analyses in parallel, providing association, dissociation, and affinity constants for several antibodies or supernatants simultaneously in one experiment. We show that the ProteOn XPR36 system is a valuable tool for use across multiple stages of the therapeutic antibody discovery and development process, enabling efficient and rapid screening after panning, affinity maturation, assay validation, and clone selection.</description><identifier>ISSN: 0003-2697</identifier><identifier>EISSN: 1096-0309</identifier><identifier>DOI: 10.1016/j.ab.2010.07.005</identifier><identifier>PMID: 20624370</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Antibodies ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - therapeutic use ; Antibody Affinity - immunology ; Antigens - immunology ; Biosensing Techniques - instrumentation ; Biosensing Techniques - methods ; CHO Cells ; Clone Cells ; Cricetinae ; Cricetulus ; High-throughput screening ; Humans ; Immunoglobulin Fab Fragments - immunology ; Immunoglobulin G - immunology ; Kinetics ; Mutation - genetics ; Phage display ; Protein Binding ; ProteOn XPR36 ; Receptors, IgG - immunology ; Reproducibility of Results ; SPR</subject><ispartof>Analytical biochemistry, 2010-11, Vol.406 (2), p.147-156</ispartof><rights>2010 Elsevier Inc.</rights><rights>Copyright 2010 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-20ce2a37258f4da96257cc7af5e1c9897ead37af33298233b2f7b955644dad153</citedby><cites>FETCH-LOGICAL-c381t-20ce2a37258f4da96257cc7af5e1c9897ead37af33298233b2f7b955644dad153</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0003269710004380$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20624370$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bronner, Vered</creatorcontrib><creatorcontrib>Denkberg, Galit</creatorcontrib><creatorcontrib>Peled, Mira</creatorcontrib><creatorcontrib>Elbaz, Yael</creatorcontrib><creatorcontrib>Zahavi, Efrat</creatorcontrib><creatorcontrib>Kasoto, Harel</creatorcontrib><creatorcontrib>Reiter, Yoram</creatorcontrib><creatorcontrib>Notcovich, Ariel</creatorcontrib><creatorcontrib>Bravman, Tsafrir</creatorcontrib><title>Therapeutic antibodies: Discovery and development using the ProteOn XPR36 biosensor interaction array system</title><title>Analytical biochemistry</title><addtitle>Anal Biochem</addtitle><description>Therapeutic monoclonal antibodies are becoming a significant and rapidly growing class of therapeutic pharmaceuticals. Their discovery and development requires fast and high-throughput methodologies for screening and selecting appropriate candidate antibodies having high affinity for the target as well as high specificity and low cross-reactivity. This study demonstrates the use of the ProteOn XPR36 protein interaction array system and its novel approach, termed One-Shot Kinetics, for the rapid screening and selection of high-affinity antibodies. This approach allows multiple quantitative protein binding analyses in parallel, providing association, dissociation, and affinity constants for several antibodies or supernatants simultaneously in one experiment. We show that the ProteOn XPR36 system is a valuable tool for use across multiple stages of the therapeutic antibody discovery and development process, enabling efficient and rapid screening after panning, affinity maturation, assay validation, and clone selection.</description><subject>Animals</subject><subject>Antibodies</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - therapeutic use</subject><subject>Antibody Affinity - immunology</subject><subject>Antigens - immunology</subject><subject>Biosensing Techniques - instrumentation</subject><subject>Biosensing Techniques - methods</subject><subject>CHO Cells</subject><subject>Clone Cells</subject><subject>Cricetinae</subject><subject>Cricetulus</subject><subject>High-throughput screening</subject><subject>Humans</subject><subject>Immunoglobulin Fab Fragments - immunology</subject><subject>Immunoglobulin G - immunology</subject><subject>Kinetics</subject><subject>Mutation - genetics</subject><subject>Phage display</subject><subject>Protein Binding</subject><subject>ProteOn XPR36</subject><subject>Receptors, IgG - immunology</subject><subject>Reproducibility of Results</subject><subject>SPR</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1r3DAQxUVpaTZp7z0V3XrydiRZlp1bST9SCCSUFHoTsjRutNjSVpIX9r-vwqa9lZ6GGX7vwbxHyBsGWwase7_bmnHLoa6gtgDyGdkwGLoGBAzPyQYARMO7QZ2R85x3AIy1sntJzjh0vBUKNmS-f8Bk9rgWb6kJxY_RecyX9KPPNh4wHevVUYcHnON-wVDomn34ScsD0rsUC94G-uPum-jo6GPGkGOiPpRqaouPgZqUzJHmYy64vCIvJjNnfP00L8j3z5_ur66bm9svX68-3DRW9Kw0HCxyIxSX_dQ6M3RcKmuVmSQyO_SDQuNEXYXgQ8-FGPmkxkHKrq20Y1JckHcn332Kv1bMRS_1G5xnEzCuWfe9BNky2f6XVLIFJnuhKgkn0qaYc8JJ75NfTDpqBvqxDL3TZtSPZWhQupZRJW-fzNdxQfdX8Cf9ClyeAKxhHDwmna3HYNH5hLZoF_2_3X8DSweZzw</recordid><startdate>20101115</startdate><enddate>20101115</enddate><creator>Bronner, Vered</creator><creator>Denkberg, Galit</creator><creator>Peled, Mira</creator><creator>Elbaz, Yael</creator><creator>Zahavi, Efrat</creator><creator>Kasoto, Harel</creator><creator>Reiter, Yoram</creator><creator>Notcovich, Ariel</creator><creator>Bravman, Tsafrir</creator><general>Elsevier Inc</general><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>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>20101115</creationdate><title>Therapeutic antibodies: Discovery and development using the ProteOn XPR36 biosensor interaction array system</title><author>Bronner, Vered ; Denkberg, Galit ; Peled, Mira ; Elbaz, Yael ; Zahavi, Efrat ; Kasoto, Harel ; Reiter, Yoram ; Notcovich, Ariel ; Bravman, Tsafrir</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-20ce2a37258f4da96257cc7af5e1c9897ead37af33298233b2f7b955644dad153</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Antibodies</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - therapeutic use</topic><topic>Antibody Affinity - immunology</topic><topic>Antigens - immunology</topic><topic>Biosensing Techniques - instrumentation</topic><topic>Biosensing Techniques - methods</topic><topic>CHO Cells</topic><topic>Clone Cells</topic><topic>Cricetinae</topic><topic>Cricetulus</topic><topic>High-throughput screening</topic><topic>Humans</topic><topic>Immunoglobulin Fab Fragments - immunology</topic><topic>Immunoglobulin G - immunology</topic><topic>Kinetics</topic><topic>Mutation - genetics</topic><topic>Phage display</topic><topic>Protein Binding</topic><topic>ProteOn XPR36</topic><topic>Receptors, IgG - immunology</topic><topic>Reproducibility of Results</topic><topic>SPR</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bronner, Vered</creatorcontrib><creatorcontrib>Denkberg, Galit</creatorcontrib><creatorcontrib>Peled, Mira</creatorcontrib><creatorcontrib>Elbaz, Yael</creatorcontrib><creatorcontrib>Zahavi, Efrat</creatorcontrib><creatorcontrib>Kasoto, Harel</creatorcontrib><creatorcontrib>Reiter, Yoram</creatorcontrib><creatorcontrib>Notcovich, Ariel</creatorcontrib><creatorcontrib>Bravman, Tsafrir</creatorcontrib><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>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bronner, Vered</au><au>Denkberg, Galit</au><au>Peled, Mira</au><au>Elbaz, Yael</au><au>Zahavi, Efrat</au><au>Kasoto, Harel</au><au>Reiter, Yoram</au><au>Notcovich, Ariel</au><au>Bravman, Tsafrir</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Therapeutic antibodies: Discovery and development using the ProteOn XPR36 biosensor interaction array system</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2010-11-15</date><risdate>2010</risdate><volume>406</volume><issue>2</issue><spage>147</spage><epage>156</epage><pages>147-156</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>Therapeutic monoclonal antibodies are becoming a significant and rapidly growing class of therapeutic pharmaceuticals. Their discovery and development requires fast and high-throughput methodologies for screening and selecting appropriate candidate antibodies having high affinity for the target as well as high specificity and low cross-reactivity. This study demonstrates the use of the ProteOn XPR36 protein interaction array system and its novel approach, termed One-Shot Kinetics, for the rapid screening and selection of high-affinity antibodies. This approach allows multiple quantitative protein binding analyses in parallel, providing association, dissociation, and affinity constants for several antibodies or supernatants simultaneously in one experiment. 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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Animals Antibodies Antibodies, Monoclonal - immunology Antibodies, Monoclonal - therapeutic use Antibody Affinity - immunology Antigens - immunology Biosensing Techniques - instrumentation Biosensing Techniques - methods CHO Cells Clone Cells Cricetinae Cricetulus High-throughput screening Humans Immunoglobulin Fab Fragments - immunology Immunoglobulin G - immunology Kinetics Mutation - genetics Phage display Protein Binding ProteOn XPR36 Receptors, IgG - immunology Reproducibility of Results SPR |
| title | Therapeutic antibodies: Discovery and development using the ProteOn XPR36 biosensor interaction array system |
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