File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: A bifunctional amino acid to study protein–protein interactions

TitleA bifunctional amino acid to study protein–protein interactions
Authors
Issue Date2020
PublisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at http://pubs.rsc.org/en/journals/journalissues/ra
Citation
RSC Advances, 2020, v. 10 n. 69, p. 42076-42083 How to Cite?
AbstractProtein–protein interactions (PPIs) play crucial roles in regulating essentially all cellular processes. Photo-cross-linking represents a powerful method to study PPIs. To fulfil the requirements for the exploration of different PPIs, there is a continuous demand on the development of novel photo-reactive amino acids with diverse structural properties and functionalities. Reported herein is the development of a bifunctional amino acid termed dzANA, which contains a diazirine, for photo-cross-linking, and a terminal alkyne group, for bioorthogonal tagging. Using known PPIs between histone posttranslational modifications (PTMs) and their binding partners as models, we demonstrate that the dzANA-harbouring peptide-based photoaffinity probes could efficiently and selectively capture the weak and transient PPIs mediated by histone modifications. Our study indicates the potential of dzANA to identify and characterize unknown PPIs.
Persistent Identifierhttp://hdl.handle.net/10722/306485
ISSN
2023 Impact Factor: 3.9
2023 SCImago Journal Rankings: 0.715
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, T-
dc.contributor.authorLi, X-
dc.contributor.authorLi, XD-
dc.date.accessioned2021-10-22T07:35:17Z-
dc.date.available2021-10-22T07:35:17Z-
dc.date.issued2020-
dc.identifier.citationRSC Advances, 2020, v. 10 n. 69, p. 42076-42083-
dc.identifier.issn2046-2069-
dc.identifier.urihttp://hdl.handle.net/10722/306485-
dc.description.abstractProtein–protein interactions (PPIs) play crucial roles in regulating essentially all cellular processes. Photo-cross-linking represents a powerful method to study PPIs. To fulfil the requirements for the exploration of different PPIs, there is a continuous demand on the development of novel photo-reactive amino acids with diverse structural properties and functionalities. Reported herein is the development of a bifunctional amino acid termed dzANA, which contains a diazirine, for photo-cross-linking, and a terminal alkyne group, for bioorthogonal tagging. Using known PPIs between histone posttranslational modifications (PTMs) and their binding partners as models, we demonstrate that the dzANA-harbouring peptide-based photoaffinity probes could efficiently and selectively capture the weak and transient PPIs mediated by histone modifications. Our study indicates the potential of dzANA to identify and characterize unknown PPIs.-
dc.languageeng-
dc.publisherRoyal Society of Chemistry: Open Access Journals. The Journal's web site is located at http://pubs.rsc.org/en/journals/journalissues/ra-
dc.relation.ispartofRSC Advances-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleA bifunctional amino acid to study protein–protein interactions-
dc.typeArticle-
dc.identifier.emailLi, X: lx418@hku.hk-
dc.identifier.emailLi, XD: xiangli@hku.hk-
dc.identifier.authorityLi, XD=rp01562-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1039/D0RA09110C-
dc.identifier.scopuseid_2-s2.0-85097129871-
dc.identifier.hkuros329010-
dc.identifier.volume10-
dc.identifier.issue69-
dc.identifier.spage42076-
dc.identifier.epage42083-
dc.identifier.isiWOS:000592897600012-
dc.publisher.placeUnited Kingdom-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats