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Single-molecule recognition of biomolecular interaction via Kelvin probe force microscopy

DC Field Value Language
dc.contributor.author양재문-
dc.contributor.author허용민-
dc.date.accessioned2014-12-20T16:54:48Z-
dc.date.available2014-12-20T16:54:48Z-
dc.date.issued2011-
dc.identifier.issn1936-0851-
dc.identifier.urihttps://ir.ymlib.yonsei.ac.kr/handle/22282913/93616-
dc.description.abstractWe report the scanning probe microscope (SPM)-based single-molecule recognition of biomolecular interactions between protein kinase and small ligands (i.e., ATP and Imatinib). In general, it is difficult to sense and detect the small ligands bound to protein kinase (at single-molecule resolution) using a conventional atomic force microscope (AFM) due to the limited resolution of conventional AFM for detecting the miniscule changes in molecular size driven by ligand binding. In this study, we have demonstrated that Kelvin probe force microscopy (KPFM) is able to articulate the surface potential of biomolecules interacting with ligands (i.e., the protein kinase-ATP interactions and inhibition phenomena induced by antagonistic molecules) in a label-free manner. Furthermore, measured surface potentials for biomolecular interactions enable quantitative descriptions on the ability of protein kinase to interact with small ligands such as ATP or antagonistic molecules. Our study sheds light on KPFM that allows the precise recognition of single-molecule interactions, which opens a new avenue for the design and development of novel molecular therapeutics.-
dc.description.statementOfResponsibilityopen-
dc.format.extent6981~6990-
dc.relation.isPartOfACS NANO-
dc.rightsCC BY-NC-ND 2.0 KR-
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/2.0/kr/-
dc.subject.MESHMicroscopy, Scanning Probe/methods*-
dc.subject.MESHProtein-Tyrosine Kinases/metabolism-
dc.titleSingle-molecule recognition of biomolecular interaction via Kelvin probe force microscopy-
dc.typeArticle-
dc.contributor.collegeResearcher Institutes (부설 연구소)-
dc.contributor.departmentYonsei Integrative Research Institute for Cerebral & Cardiovascular Disease (뇌심혈관질환융합연구사업단)-
dc.contributor.googleauthorJinsung Park-
dc.contributor.googleauthorJaemoon Yang-
dc.contributor.googleauthorGyudo Lee-
dc.contributor.googleauthorChang Young Lee-
dc.contributor.googleauthorSungsoo Na-
dc.contributor.googleauthorSang Woo Lee-
dc.contributor.googleauthorSeungjoo Haam-
dc.contributor.googleauthorYong-Min Huh-
dc.contributor.googleauthorDae Sung Yoon-
dc.contributor.googleauthorKilho Eom-
dc.contributor.googleauthorTaeyun Kwon-
dc.identifier.doi10.1021/nn201540c-
dc.admin.authorfalse-
dc.admin.mappingfalse-
dc.contributor.localIdA04359-
dc.contributor.localIdA02315-
dc.relation.journalcodeJ00005-
dc.identifier.eissn1936-086X-
dc.identifier.pmid21806048-
dc.identifier.urlhttp://pubs.acs.org/doi/abs/10.1021/nn201540c-
dc.subject.keywordbiomolecular interactions-
dc.subject.keywordKelvin probe force microscopy-
dc.subject.keywordlabel-free-
dc.subject.keywordprotein kinase-
dc.subject.keywordsingle molecule-
dc.subject.keywordsurface potential-
dc.contributor.alternativeNameYang, Jae Moon-
dc.contributor.alternativeNameHuh, Yong Min-
dc.contributor.affiliatedAuthorHuh, Yong Min-
dc.contributor.affiliatedAuthorYang, Jae Moon-
dc.rights.accessRightsnot free-
dc.citation.volume5-
dc.citation.number9-
dc.citation.startPage6981-
dc.citation.endPage6990-
dc.identifier.bibliographicCitationACS NANO, Vol.5(9) : 6981-6990, 2011-
dc.identifier.rimsid28343-
dc.type.rimsART-
Appears in Collections:
1. College of Medicine (의과대학) > Research Institute (부설연구소) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Radiology (영상의학교실) > 1. Journal Papers

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