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Article: Multivalent Photoaffinity Probe for Labeling Small Molecule Binding Proteins

TitleMultivalent Photoaffinity Probe for Labeling Small Molecule Binding Proteins
Authors
Issue Date2014
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/bc
Citation
Bioconjugate Chemistry, 2014, v. 25 n. 6, p. 1172-1180 How to Cite?
AbstractCharacterization of small molecule (SM)-protein interaction is of high importance in biomedical research such as target identification and proteomic profiling. Photo-cross-linking is a powerful and straightforward strategy to covalently capture SM's binding proteins. The DNA-based photoaffinity labeling method is able to capture SM's protein targets with high specificity but suffers low cross-linking efficiency, which limits its utility for low abundance and low affinity proteins. After screening a variety of cross-linkers, by utilizing the multivalency effect, the cross-linking efficiency was improved by nearly 7-fold without compromising probe specificity. The generality and performance of multivalent photoaffinity probes have been validated with a variety of SM-protein pairs in the complexity of cell lysates. © 2014 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/221118
ISSN
2015 Impact Factor: 4.5
2015 SCImago Journal Rankings: 1.754
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLi, G-
dc.contributor.authorLiu, Y-
dc.contributor.authorYu, XR-
dc.contributor.authorLi, X-
dc.date.accessioned2015-10-27T08:48:26Z-
dc.date.available2015-10-27T08:48:26Z-
dc.date.issued2014-
dc.identifier.citationBioconjugate Chemistry, 2014, v. 25 n. 6, p. 1172-1180-
dc.identifier.issn1043-1802-
dc.identifier.urihttp://hdl.handle.net/10722/221118-
dc.description.abstractCharacterization of small molecule (SM)-protein interaction is of high importance in biomedical research such as target identification and proteomic profiling. Photo-cross-linking is a powerful and straightforward strategy to covalently capture SM's binding proteins. The DNA-based photoaffinity labeling method is able to capture SM's protein targets with high specificity but suffers low cross-linking efficiency, which limits its utility for low abundance and low affinity proteins. After screening a variety of cross-linkers, by utilizing the multivalency effect, the cross-linking efficiency was improved by nearly 7-fold without compromising probe specificity. The generality and performance of multivalent photoaffinity probes have been validated with a variety of SM-protein pairs in the complexity of cell lysates. © 2014 American Chemical Society.-
dc.languageeng-
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/bc-
dc.relation.ispartofBioconjugate Chemistry-
dc.titleMultivalent Photoaffinity Probe for Labeling Small Molecule Binding Proteins-
dc.typeArticle-
dc.identifier.emailLi, X: xiaoyuli@hku.hk-
dc.identifier.authorityLi, X=rp02080-
dc.identifier.doi10.1021/bc500195w-
dc.identifier.pmid24849297-
dc.identifier.scopuseid_2-s2.0-84902655650-
dc.identifier.volume25-
dc.identifier.issue6-
dc.identifier.spage1172-
dc.identifier.epage1180-
dc.identifier.isiWOS:000337720000017-
dc.publisher.placeUnited States-

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