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Article: Detecting CD20-Rituximab interaction forces using AFM single-molecule force spectroscopy

TitleDetecting CD20-Rituximab interaction forces using AFM single-molecule force spectroscopy
Authors
Keywordsnon-Hodgkin's lymphoma
atomic force microscopy
single-molecule force spectroscopy
monoclonal antibody
Issue Date2011
Citation
Chinese Science Bulletin, 2011, v. 56, n. 35, p. 3829-3835 How to Cite?
AbstractThe invention of atomic force microscopy (AFM) has provided new technology for measuring specific molecular interaction forces. Using AFM single-molecule force spectroscopy (SMFS) techniques, CD20-Rituximab rupture forces were measured on purified CD20 proteins, Raji cells, and lymphoma patient B cells. Rituximab molecules were linked onto AFM tips using AFM probe functionalization technology, and purified CD20 proteins were attached to mica using substrate functionalization technology. Raji cells (a lymphoma cell line) or lymphoma patient cells were immobilized on a glass substrate via electrostatic adsorption and chemical fixation. The topography of the purified CD20 proteins, Raji cells, and patient lymphoma cells was visualized using AFM imaging and the differences in the rupture forces were analyzed and measured. The results showed that the rupture forces between the CD20 proteins on Raji cells and Rituximab were markedly smaller than those for purified CD20 proteins and CD20 proteins on lymphoma patient B cells. These findings provide an effective experimental method for investigating the mechanisms underlying the variable efficacy of Rituximab. © 2011 Science China Press and Springer-Verlag Berlin Heidelberg.
Persistent Identifierhttp://hdl.handle.net/10722/213211
ISSN
2015 Impact Factor: 1.789

 

DC FieldValueLanguage
dc.contributor.authorLi, Mi-
dc.contributor.authorLiu, Lian Qing-
dc.contributor.authorXi, Ning-
dc.contributor.authorWang, Yue Chao-
dc.contributor.authorDong, Zai Li-
dc.contributor.authorLi, Guang Yong-
dc.contributor.authorXiao, Xiu Bin-
dc.contributor.authorZhang, Wei Jing-
dc.date.accessioned2015-07-28T04:06:32Z-
dc.date.available2015-07-28T04:06:32Z-
dc.date.issued2011-
dc.identifier.citationChinese Science Bulletin, 2011, v. 56, n. 35, p. 3829-3835-
dc.identifier.issn1001-6538-
dc.identifier.urihttp://hdl.handle.net/10722/213211-
dc.description.abstractThe invention of atomic force microscopy (AFM) has provided new technology for measuring specific molecular interaction forces. Using AFM single-molecule force spectroscopy (SMFS) techniques, CD20-Rituximab rupture forces were measured on purified CD20 proteins, Raji cells, and lymphoma patient B cells. Rituximab molecules were linked onto AFM tips using AFM probe functionalization technology, and purified CD20 proteins were attached to mica using substrate functionalization technology. Raji cells (a lymphoma cell line) or lymphoma patient cells were immobilized on a glass substrate via electrostatic adsorption and chemical fixation. The topography of the purified CD20 proteins, Raji cells, and patient lymphoma cells was visualized using AFM imaging and the differences in the rupture forces were analyzed and measured. The results showed that the rupture forces between the CD20 proteins on Raji cells and Rituximab were markedly smaller than those for purified CD20 proteins and CD20 proteins on lymphoma patient B cells. These findings provide an effective experimental method for investigating the mechanisms underlying the variable efficacy of Rituximab. © 2011 Science China Press and Springer-Verlag Berlin Heidelberg.-
dc.languageeng-
dc.relation.ispartofChinese Science Bulletin-
dc.subjectnon-Hodgkin's lymphoma-
dc.subjectatomic force microscopy-
dc.subjectsingle-molecule force spectroscopy-
dc.subjectmonoclonal antibody-
dc.titleDetecting CD20-Rituximab interaction forces using AFM single-molecule force spectroscopy-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s11434-011-4789-0-
dc.identifier.scopuseid_2-s2.0-82555178530-
dc.identifier.volume56-
dc.identifier.issue35-
dc.identifier.spage3829-
dc.identifier.epage3835-
dc.identifier.eissn1861-9541-

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