Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins
The dynamic strength of multiple specific bonds exposed to external mechanical force is of significant interest for the understanding of biological adhesion. Exploiting the well-established FLAG tag technology, we engineered model proteins exhibiting no, one, or two identical binding sites for a mon...
Gespeichert in:
Veröffentlicht in: | The journal of physical chemistry. B 2011-03, Vol.115 (11), p.2582-2592 |
---|---|
Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 2592 |
---|---|
container_issue | 11 |
container_start_page | 2582 |
container_title | The journal of physical chemistry. B |
container_volume | 115 |
creator | Loritz, H.-M Kirchgessner, N Born, S Hoffmann, B Merkel, R |
description | The dynamic strength of multiple specific bonds exposed to external mechanical force is of significant interest for the understanding of biological adhesion. Exploiting the well-established FLAG tag technology, we engineered model proteins exhibiting no, one, or two identical binding sites for a monoclonal antibody. Bonds between these engineered proteins and the antibody were studied with dynamic force spectroscopy. On single bonds between a FLAG-tag and the antibody, we observed two regimes corresponding to two different activated complexes, that is, two intermediate states along the reaction path for bond breakage. Dynamic force spectroscopy on double bonds showed the same two regimes. The actual yield forces of double bonds slightly exceeded those of single bonds. A simplified kinetic model with analytical solutions was developed and used to interpret the measured spectra. |
doi_str_mv | 10.1021/jp108280q |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_857811436</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>857811436</sourcerecordid><originalsourceid>FETCH-LOGICAL-a314t-7ed54eead84d10b7ce39ca6f9de647698c3b6b137a5993c0a6eb92db62e34c393</originalsourceid><addsrcrecordid>eNpt0L1OwzAUBWALgWj5GXgB5AUhhoAdx07CVqoClYqoVJgjx75pXaV2aidD356glk4M1vXw3SPdg9ANJY-UxPRp3VCSxRnZnqAh5TGJ-peeHv6CEjFAFyGsCYl5nIlzNIgp41wQPkTVB6iVtEbJGi9aD3bZrrCr8KIBZSqj8IuzOuCRao1d4mlwtWxBY-exsXgujQ_PeITHMkC_3ukddhZP7NJYAN-7uXctGBuu0Fkl6wDXh3mJvl8nX-P3aPb5Nh2PZpFkNGmjFDRPAKTOEk1JmSpguZKiyjWIJBV5plgpSspSyfOcKSIFlHmsSxEDSxTL2SW63-c23m07CG2xMUFBXUsLrgtFxtOM0oSJXj7spfIuBA9V0XizkX5XUFL8tlocW-3t7SG1Kzegj_Kvxh7c7YFUoVi7ztv-yH-CfgBUyn3-</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>857811436</pqid></control><display><type>article</type><title>Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Loritz, H.-M ; Kirchgessner, N ; Born, S ; Hoffmann, B ; Merkel, R</creator><creatorcontrib>Loritz, H.-M ; Kirchgessner, N ; Born, S ; Hoffmann, B ; Merkel, R</creatorcontrib><description>The dynamic strength of multiple specific bonds exposed to external mechanical force is of significant interest for the understanding of biological adhesion. Exploiting the well-established FLAG tag technology, we engineered model proteins exhibiting no, one, or two identical binding sites for a monoclonal antibody. Bonds between these engineered proteins and the antibody were studied with dynamic force spectroscopy. On single bonds between a FLAG-tag and the antibody, we observed two regimes corresponding to two different activated complexes, that is, two intermediate states along the reaction path for bond breakage. Dynamic force spectroscopy on double bonds showed the same two regimes. The actual yield forces of double bonds slightly exceeded those of single bonds. A simplified kinetic model with analytical solutions was developed and used to interpret the measured spectra.</description><identifier>ISSN: 1520-6106</identifier><identifier>EISSN: 1520-5207</identifier><identifier>DOI: 10.1021/jp108280q</identifier><identifier>PMID: 21355605</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Algorithms ; Antibodies, Monoclonal - chemistry ; Antibodies, Monoclonal - immunology ; Antibody Affinity ; B: Biophysical Chemistry ; Biomechanical Phenomena ; Green Fluorescent Proteins - genetics ; Kinetics ; Models, Chemical ; Oligopeptides ; Peptides - chemistry ; Peptides - genetics ; Peptides - immunology ; Probability ; Protein Binding ; Protein Engineering ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Spectrum Analysis - methods ; Statistical Distributions</subject><ispartof>The journal of physical chemistry. B, 2011-03, Vol.115 (11), p.2582-2592</ispartof><rights>Copyright © 2011 American Chemical Society</rights><rights>2011 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a314t-7ed54eead84d10b7ce39ca6f9de647698c3b6b137a5993c0a6eb92db62e34c393</citedby><cites>FETCH-LOGICAL-a314t-7ed54eead84d10b7ce39ca6f9de647698c3b6b137a5993c0a6eb92db62e34c393</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/jp108280q$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jp108280q$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,2765,27076,27924,27925,56738,56788</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21355605$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Loritz, H.-M</creatorcontrib><creatorcontrib>Kirchgessner, N</creatorcontrib><creatorcontrib>Born, S</creatorcontrib><creatorcontrib>Hoffmann, B</creatorcontrib><creatorcontrib>Merkel, R</creatorcontrib><title>Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins</title><title>The journal of physical chemistry. B</title><addtitle>J. Phys. Chem. B</addtitle><description>The dynamic strength of multiple specific bonds exposed to external mechanical force is of significant interest for the understanding of biological adhesion. Exploiting the well-established FLAG tag technology, we engineered model proteins exhibiting no, one, or two identical binding sites for a monoclonal antibody. Bonds between these engineered proteins and the antibody were studied with dynamic force spectroscopy. On single bonds between a FLAG-tag and the antibody, we observed two regimes corresponding to two different activated complexes, that is, two intermediate states along the reaction path for bond breakage. Dynamic force spectroscopy on double bonds showed the same two regimes. The actual yield forces of double bonds slightly exceeded those of single bonds. A simplified kinetic model with analytical solutions was developed and used to interpret the measured spectra.</description><subject>Algorithms</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity</subject><subject>B: Biophysical Chemistry</subject><subject>Biomechanical Phenomena</subject><subject>Green Fluorescent Proteins - genetics</subject><subject>Kinetics</subject><subject>Models, Chemical</subject><subject>Oligopeptides</subject><subject>Peptides - chemistry</subject><subject>Peptides - genetics</subject><subject>Peptides - immunology</subject><subject>Probability</subject><subject>Protein Binding</subject><subject>Protein Engineering</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Spectrum Analysis - methods</subject><subject>Statistical Distributions</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0L1OwzAUBWALgWj5GXgB5AUhhoAdx07CVqoClYqoVJgjx75pXaV2aidD356glk4M1vXw3SPdg9ANJY-UxPRp3VCSxRnZnqAh5TGJ-peeHv6CEjFAFyGsCYl5nIlzNIgp41wQPkTVB6iVtEbJGi9aD3bZrrCr8KIBZSqj8IuzOuCRao1d4mlwtWxBY-exsXgujQ_PeITHMkC_3ukddhZP7NJYAN-7uXctGBuu0Fkl6wDXh3mJvl8nX-P3aPb5Nh2PZpFkNGmjFDRPAKTOEk1JmSpguZKiyjWIJBV5plgpSspSyfOcKSIFlHmsSxEDSxTL2SW63-c23m07CG2xMUFBXUsLrgtFxtOM0oSJXj7spfIuBA9V0XizkX5XUFL8tlocW-3t7SG1Kzegj_Kvxh7c7YFUoVi7ztv-yH-CfgBUyn3-</recordid><startdate>20110324</startdate><enddate>20110324</enddate><creator>Loritz, H.-M</creator><creator>Kirchgessner, N</creator><creator>Born, S</creator><creator>Hoffmann, B</creator><creator>Merkel, R</creator><general>American Chemical Society</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></search><sort><creationdate>20110324</creationdate><title>Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins</title><author>Loritz, H.-M ; Kirchgessner, N ; Born, S ; Hoffmann, B ; Merkel, R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a314t-7ed54eead84d10b7ce39ca6f9de647698c3b6b137a5993c0a6eb92db62e34c393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Algorithms</topic><topic>Antibodies, Monoclonal - chemistry</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibody Affinity</topic><topic>B: Biophysical Chemistry</topic><topic>Biomechanical Phenomena</topic><topic>Green Fluorescent Proteins - genetics</topic><topic>Kinetics</topic><topic>Models, Chemical</topic><topic>Oligopeptides</topic><topic>Peptides - chemistry</topic><topic>Peptides - genetics</topic><topic>Peptides - immunology</topic><topic>Probability</topic><topic>Protein Binding</topic><topic>Protein Engineering</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Spectrum Analysis - methods</topic><topic>Statistical Distributions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Loritz, H.-M</creatorcontrib><creatorcontrib>Kirchgessner, N</creatorcontrib><creatorcontrib>Born, S</creatorcontrib><creatorcontrib>Hoffmann, B</creatorcontrib><creatorcontrib>Merkel, R</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><jtitle>The journal of physical chemistry. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Loritz, H.-M</au><au>Kirchgessner, N</au><au>Born, S</au><au>Hoffmann, B</au><au>Merkel, R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins</atitle><jtitle>The journal of physical chemistry. B</jtitle><addtitle>J. Phys. Chem. B</addtitle><date>2011-03-24</date><risdate>2011</risdate><volume>115</volume><issue>11</issue><spage>2582</spage><epage>2592</epage><pages>2582-2592</pages><issn>1520-6106</issn><eissn>1520-5207</eissn><abstract>The dynamic strength of multiple specific bonds exposed to external mechanical force is of significant interest for the understanding of biological adhesion. Exploiting the well-established FLAG tag technology, we engineered model proteins exhibiting no, one, or two identical binding sites for a monoclonal antibody. Bonds between these engineered proteins and the antibody were studied with dynamic force spectroscopy. On single bonds between a FLAG-tag and the antibody, we observed two regimes corresponding to two different activated complexes, that is, two intermediate states along the reaction path for bond breakage. Dynamic force spectroscopy on double bonds showed the same two regimes. The actual yield forces of double bonds slightly exceeded those of single bonds. A simplified kinetic model with analytical solutions was developed and used to interpret the measured spectra.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>21355605</pmid><doi>10.1021/jp108280q</doi><tpages>11</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1520-6106 |
ispartof | The journal of physical chemistry. B, 2011-03, Vol.115 (11), p.2582-2592 |
issn | 1520-6106 1520-5207 |
language | eng |
recordid | cdi_proquest_miscellaneous_857811436 |
source | MEDLINE; American Chemical Society Journals |
subjects | Algorithms Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - immunology Antibody Affinity B: Biophysical Chemistry Biomechanical Phenomena Green Fluorescent Proteins - genetics Kinetics Models, Chemical Oligopeptides Peptides - chemistry Peptides - genetics Peptides - immunology Probability Protein Binding Protein Engineering Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - immunology Spectrum Analysis - methods Statistical Distributions |
title | Mechanical Strength of Specific Bonds Acting Isolated or in Pairs: A Case Study on Engineered Proteins |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T00%3A56%3A34IST&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=Mechanical%20Strength%20of%20Specific%20Bonds%20Acting%20Isolated%20or%20in%20Pairs:%20A%20Case%20Study%20on%20Engineered%20Proteins&rft.jtitle=The%20journal%20of%20physical%20chemistry.%20B&rft.au=Loritz,%20H.-M&rft.date=2011-03-24&rft.volume=115&rft.issue=11&rft.spage=2582&rft.epage=2592&rft.pages=2582-2592&rft.issn=1520-6106&rft.eissn=1520-5207&rft_id=info:doi/10.1021/jp108280q&rft_dat=%3Cproquest_cross%3E857811436%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=857811436&rft_id=info:pmid/21355605&rfr_iscdi=true |