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dc.contributor.authorMurale, Dhiraj P.-
dc.contributor.authorHong, Seong Cheol-
dc.contributor.authorJang, Se-young-
dc.contributor.authorLee, Jun-Seok-
dc.date.accessioned2024-01-19T21:03:55Z-
dc.date.available2024-01-19T21:03:55Z-
dc.date.created2021-09-04-
dc.date.issued2018-12-18-
dc.identifier.issn1439-4227-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/120564-
dc.description.abstractMany intracellular proteins are metabolically unstable, and their half-life was known to be controlled by the "N-end rule," that is, the N-terminal residue controlled protein stability. To visualize or measure the cellular stability of a protein, depending on the N-terminal residues, attention is being paid to the development of selective labeling methods for individual N-terminal amino acids. However, there are only a limited number of functional groups available for specific N-terminal amino acid labeling in a biological environment. Herein, we report a re-examination of salicylaldehyde ester for selective N-terminal residue tagging. Salicylaldehyde ester has been used for chemical ligation to N-terminal serine or threonine under pyridine/acetic acid conditions. Inspired by previous selective serine/threonine labeling, N-terminal labeling of salicylaldehyde ester in aqueous buffer has been examined by using boron-dipyrromethene (BODIPY), rhodamine, and coumarin probes. Surprisingly, the selectivity not only significantly differed, depending on the fluorophore incorporated in salicylaldehyde, but was also perturbed by the addition of a small fraction of phosphate-buffered saline. In particular, the coumarin-based salicylaldehyde ester probe showed notable selectivity against N-terminal cysteine under aqueous buffer conditions. This result reveals the serendipitous discovery of a new N-terminal cysteine labeling strategy.-
dc.languageEnglish-
dc.publisherWILEY-V C H VERLAG GMBH-
dc.subjectEND RULE-
dc.subjectPROTEIN-
dc.subjectSERINE-
dc.subjectBIOCONJUGATION-
dc.subjectTHREONINE-
dc.subjectPEPTIDES-
dc.subjectLIGATION-
dc.titleReinvestigation of an O-Salicylaldehyde Ester Functional Group in Aqueous Buffer and Discovery of a Coumarin Scaffold Probe for Selective N-Terminal Cysteine Labeling-
dc.typeArticle-
dc.identifier.doi10.1002/cbic.201800565-
dc.description.journalClass1-
dc.identifier.bibliographicCitationCHEMBIOCHEM, v.19, no.24, pp.2545 - 2549-
dc.citation.titleCHEMBIOCHEM-
dc.citation.volume19-
dc.citation.number24-
dc.citation.startPage2545-
dc.citation.endPage2549-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000453835200004-
dc.identifier.scopusid2-s2.0-85056416110-
dc.relation.journalWebOfScienceCategoryBiochemistry & Molecular Biology-
dc.relation.journalWebOfScienceCategoryChemistry, Medicinal-
dc.relation.journalResearchAreaBiochemistry & Molecular Biology-
dc.relation.journalResearchAreaPharmacology & Pharmacy-
dc.type.docTypeArticle-
dc.subject.keywordPlusEND RULE-
dc.subject.keywordPlusPROTEIN-
dc.subject.keywordPlusSERINE-
dc.subject.keywordPlusBIOCONJUGATION-
dc.subject.keywordPlusTHREONINE-
dc.subject.keywordPlusPEPTIDES-
dc.subject.keywordPlusLIGATION-
dc.subject.keywordAuthoramino acids-
dc.subject.keywordAuthorfluorescence-
dc.subject.keywordAuthorlabeling agents-
dc.subject.keywordAuthorpeptides-
dc.subject.keywordAuthorsalicylaldehyde ester-
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KIST Article > 2018
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