Loading…

Biomolecular Interactions Measured by Atomic Force Microscopy

Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitati...

Full description

Saved in:
Bibliographic Details
Published in:Biophysical journal 2000-12, Vol.79 (6), p.3267-3281
Main Authors: Willemsen, Oscar H., Snel, Margot M.E., Cambi, Alessandra, Greve, Jan, De Grooth, Bart G., Figdor, Carl G.
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63
cites cdi_FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63
container_end_page 3281
container_issue 6
container_start_page 3267
container_title Biophysical journal
container_volume 79
creator Willemsen, Oscar H.
Snel, Margot M.E.
Cambi, Alessandra
Greve, Jan
De Grooth, Bart G.
Figdor, Carl G.
description Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitative. At the same time, theories have been developed to describe and understand the dynamics of the unbinding process and experimental techniques have been refined to verify this theory. In addition, the detection of molecular recognition forces has been exploited to map and image the location of binding sites. In this review we discuss the important contributions that have led to the development of this field. In addition, we emphasize the potential of chemically well-defined surface modification techniques to further improve reproducible measurements by AFM. This increased reproducibility will pave the way for a better understanding of molecular interactions in cell biology.
doi_str_mv 10.1016/S0006-3495(00)76559-3
format article
fullrecord <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1301201</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006349500765593</els_id><sourcerecordid>72462540</sourcerecordid><originalsourceid>FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63</originalsourceid><addsrcrecordid>eNqFkc1P3DAQxS0EYpePP6FV1EMFh7QzcezgQ1sBYlskVhxazpbXmVCvknixE6T978l-aKG9cPJhfvPG7z3GPiB8QUD59TcAyJTnSpwBnBdSCJXyPTZGkWcpwIXcZ-MdMmJHMc4BMBOAh2yEiCAlhzH7duV842uyfW1Cctt2FIztnG9jMiUT-0BlMlsml51vnE0mPlhKps4GH61fLE_YQWXqSKfb95g9TG7-XP9K7-5_3l5f3qVWCNmlNLNKmUqSAJhlvCxlUVIBhtQFkuIiF5wbSSAKqpQ0lSisza2SFXFTYSn5Mfu-0V30s4ZKS20XTK0XwTUmLLU3Tv87ad1f_eifNfLBM-Ag8HkrEPxTT7HTjYuW6tq05PuoiyyXmchhAD_9B859H9rBnM5QFKgAiwESG2iVQwxU7X6CoFft6HU7ehW9BtDrdjQf9j6-tfG6ta1jAH5sABrCfHYUdLSOWkulC2Q7XXr3zokXBxCfyQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>215719017</pqid></control><display><type>article</type><title>Biomolecular Interactions Measured by Atomic Force Microscopy</title><source>BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS</source><source>Open Access: PubMed Central</source><creator>Willemsen, Oscar H. ; Snel, Margot M.E. ; Cambi, Alessandra ; Greve, Jan ; De Grooth, Bart G. ; Figdor, Carl G.</creator><creatorcontrib>Willemsen, Oscar H. ; Snel, Margot M.E. ; Cambi, Alessandra ; Greve, Jan ; De Grooth, Bart G. ; Figdor, Carl G.</creatorcontrib><description>Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitative. At the same time, theories have been developed to describe and understand the dynamics of the unbinding process and experimental techniques have been refined to verify this theory. In addition, the detection of molecular recognition forces has been exploited to map and image the location of binding sites. In this review we discuss the important contributions that have led to the development of this field. In addition, we emphasize the potential of chemically well-defined surface modification techniques to further improve reproducible measurements by AFM. This increased reproducibility will pave the way for a better understanding of molecular interactions in cell biology.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(00)76559-3</identifier><identifier>PMID: 11106630</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Atoms &amp; subatomic particles ; Biophysics - methods ; Chemical bonds ; Microscopy, Atomic Force - methods ; Molecular biology ; Molecules ; Proteins - chemistry</subject><ispartof>Biophysical journal, 2000-12, Vol.79 (6), p.3267-3281</ispartof><rights>2000 The Biophysical Society</rights><rights>Copyright Biophysical Society Dec 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63</citedby><cites>FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63</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/PMC1301201/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1301201/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,733,786,790,891,27957,27958,53827,53829</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11106630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Willemsen, Oscar H.</creatorcontrib><creatorcontrib>Snel, Margot M.E.</creatorcontrib><creatorcontrib>Cambi, Alessandra</creatorcontrib><creatorcontrib>Greve, Jan</creatorcontrib><creatorcontrib>De Grooth, Bart G.</creatorcontrib><creatorcontrib>Figdor, Carl G.</creatorcontrib><title>Biomolecular Interactions Measured by Atomic Force Microscopy</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitative. At the same time, theories have been developed to describe and understand the dynamics of the unbinding process and experimental techniques have been refined to verify this theory. In addition, the detection of molecular recognition forces has been exploited to map and image the location of binding sites. In this review we discuss the important contributions that have led to the development of this field. In addition, we emphasize the potential of chemically well-defined surface modification techniques to further improve reproducible measurements by AFM. This increased reproducibility will pave the way for a better understanding of molecular interactions in cell biology.</description><subject>Atoms &amp; subatomic particles</subject><subject>Biophysics - methods</subject><subject>Chemical bonds</subject><subject>Microscopy, Atomic Force - methods</subject><subject>Molecular biology</subject><subject>Molecules</subject><subject>Proteins - chemistry</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkc1P3DAQxS0EYpePP6FV1EMFh7QzcezgQ1sBYlskVhxazpbXmVCvknixE6T978l-aKG9cPJhfvPG7z3GPiB8QUD59TcAyJTnSpwBnBdSCJXyPTZGkWcpwIXcZ-MdMmJHMc4BMBOAh2yEiCAlhzH7duV842uyfW1Cctt2FIztnG9jMiUT-0BlMlsml51vnE0mPlhKps4GH61fLE_YQWXqSKfb95g9TG7-XP9K7-5_3l5f3qVWCNmlNLNKmUqSAJhlvCxlUVIBhtQFkuIiF5wbSSAKqpQ0lSisza2SFXFTYSn5Mfu-0V30s4ZKS20XTK0XwTUmLLU3Tv87ad1f_eifNfLBM-Ag8HkrEPxTT7HTjYuW6tq05PuoiyyXmchhAD_9B859H9rBnM5QFKgAiwESG2iVQwxU7X6CoFft6HU7ehW9BtDrdjQf9j6-tfG6ta1jAH5sABrCfHYUdLSOWkulC2Q7XXr3zokXBxCfyQ</recordid><startdate>20001201</startdate><enddate>20001201</enddate><creator>Willemsen, Oscar H.</creator><creator>Snel, Margot M.E.</creator><creator>Cambi, Alessandra</creator><creator>Greve, Jan</creator><creator>De Grooth, Bart G.</creator><creator>Figdor, Carl G.</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>20001201</creationdate><title>Biomolecular Interactions Measured by Atomic Force Microscopy</title><author>Willemsen, Oscar H. ; Snel, Margot M.E. ; Cambi, Alessandra ; Greve, Jan ; De Grooth, Bart G. ; Figdor, Carl G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Atoms &amp; subatomic particles</topic><topic>Biophysics - methods</topic><topic>Chemical bonds</topic><topic>Microscopy, Atomic Force - methods</topic><topic>Molecular biology</topic><topic>Molecules</topic><topic>Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Willemsen, Oscar H.</creatorcontrib><creatorcontrib>Snel, Margot M.E.</creatorcontrib><creatorcontrib>Cambi, Alessandra</creatorcontrib><creatorcontrib>Greve, Jan</creatorcontrib><creatorcontrib>De Grooth, Bart G.</creatorcontrib><creatorcontrib>Figdor, Carl G.</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 &amp; 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>PHMC-Proquest健康医学期刊库</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)</collection><collection>ProQuest Central</collection><collection>Advanced Technologies &amp; Aerospace Database‎ (1962 - current)</collection><collection>ProQuest Agriculture &amp; Environmental Science Database</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</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 (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest research library</collection><collection>ProQuest Science Journals</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; 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>Willemsen, Oscar H.</au><au>Snel, Margot M.E.</au><au>Cambi, Alessandra</au><au>Greve, Jan</au><au>De Grooth, Bart G.</au><au>Figdor, Carl G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biomolecular Interactions Measured by Atomic Force Microscopy</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2000-12-01</date><risdate>2000</risdate><volume>79</volume><issue>6</issue><spage>3267</spage><epage>3281</epage><pages>3267-3281</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>Atomic force microscopy (AFM) is nowadays frequently applied to determine interaction forces between biological molecules. Starting with the detection of the first discrete unbinding forces between ligands and receptors by AFM only several years ago, measurements have become more and more quantitative. At the same time, theories have been developed to describe and understand the dynamics of the unbinding process and experimental techniques have been refined to verify this theory. In addition, the detection of molecular recognition forces has been exploited to map and image the location of binding sites. In this review we discuss the important contributions that have led to the development of this field. In addition, we emphasize the potential of chemically well-defined surface modification techniques to further improve reproducible measurements by AFM. This increased reproducibility will pave the way for a better understanding of molecular interactions in cell biology.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11106630</pmid><doi>10.1016/S0006-3495(00)76559-3</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0006-3495
ispartof Biophysical journal, 2000-12, Vol.79 (6), p.3267-3281
issn 0006-3495
1542-0086
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1301201
source BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS; Open Access: PubMed Central
subjects Atoms & subatomic particles
Biophysics - methods
Chemical bonds
Microscopy, Atomic Force - methods
Molecular biology
Molecules
Proteins - chemistry
title Biomolecular Interactions Measured by Atomic Force Microscopy
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-09-22T12%3A33%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Biomolecular%20Interactions%20Measured%20by%20Atomic%20Force%20Microscopy&rft.jtitle=Biophysical%20journal&rft.au=Willemsen,%20Oscar%20H.&rft.date=2000-12-01&rft.volume=79&rft.issue=6&rft.spage=3267&rft.epage=3281&rft.pages=3267-3281&rft.issn=0006-3495&rft.eissn=1542-0086&rft_id=info:doi/10.1016/S0006-3495(00)76559-3&rft_dat=%3Cproquest_pubme%3E72462540%3C/proquest_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c556t-ebc99af6e500b23dd67de70ae981e9354533a6e057ef96af57cc4c96fe3af1d63%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=215719017&rft_id=info:pmid/11106630&rfr_iscdi=true