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Book Chapter: Ortho-Phthalaldehyde (OPA)-based chemoselective protein bioconjugation and peptide cyclization

TitleOrtho-Phthalaldehyde (OPA)-based chemoselective protein bioconjugation and peptide cyclization
Authors
KeywordsProtein bioconjugation
Peptide cyclization
Biocompatible reaction
Chemoselective
Ortho-phthalaldehyde
Issue Date2020
PublisherAcademic Press.
Citation
Ortho-Phthalaldehyde (OPA)-based chemoselective protein bioconjugation and peptide cyclization. In Chenoweth, DM (Ed.), Chemical Tools for Imaging, Manipulating, and Tracking Biological Systems: Diverse Methods for Optical Imaging and Conjugation, p. 237-261. Cambridge, MA: Academic Press, 2020 How to Cite?
AbstractOrtho-Phthalaldehyde (OPA)-amine reaction and OPA-amine-thiol reaction have been developed to effectively modify native peptides and proteins under the physiological conditions. First, OPA and its derivatives can rapidly and smoothly react with primary amine moieties in peptides and proteins to achieve native protein biconjugations. Furthermore, OPA-alkyne bifunctional linkers can be used for proteome profiling. Second, OPA-amine-thiol three-component reaction has been developed for chemoselective peptide cyclization, directly on unprotected peptides in the aqueous buffer. Moreover, this OPA-guided cyclic peptide can be further modified with the N-maleimide moiety in one pot to introduce additional functionalities. The development of this OPA based chemoselective bioconjugation and peptide cyclization extends the toolbox for protein chemical modification and construction of cyclic peptides.
Persistent Identifierhttp://hdl.handle.net/10722/285048
ISBN
ISSN
2019 Impact Factor: 1.394
2015 SCImago Journal Rankings: 1.501
ISI Accession Number ID
Series/Report no.Methods in Enzymology ; 639

 

DC FieldValueLanguage
dc.contributor.authorZhang, Q-
dc.contributor.authorZhang, Y-
dc.contributor.authorLi, X-
dc.date.accessioned2020-08-07T09:06:02Z-
dc.date.available2020-08-07T09:06:02Z-
dc.date.issued2020-
dc.identifier.citationOrtho-Phthalaldehyde (OPA)-based chemoselective protein bioconjugation and peptide cyclization. In Chenoweth, DM (Ed.), Chemical Tools for Imaging, Manipulating, and Tracking Biological Systems: Diverse Methods for Optical Imaging and Conjugation, p. 237-261. Cambridge, MA: Academic Press, 2020-
dc.identifier.isbn9780128211519-
dc.identifier.issn0076-6879-
dc.identifier.urihttp://hdl.handle.net/10722/285048-
dc.description.abstractOrtho-Phthalaldehyde (OPA)-amine reaction and OPA-amine-thiol reaction have been developed to effectively modify native peptides and proteins under the physiological conditions. First, OPA and its derivatives can rapidly and smoothly react with primary amine moieties in peptides and proteins to achieve native protein biconjugations. Furthermore, OPA-alkyne bifunctional linkers can be used for proteome profiling. Second, OPA-amine-thiol three-component reaction has been developed for chemoselective peptide cyclization, directly on unprotected peptides in the aqueous buffer. Moreover, this OPA-guided cyclic peptide can be further modified with the N-maleimide moiety in one pot to introduce additional functionalities. The development of this OPA based chemoselective bioconjugation and peptide cyclization extends the toolbox for protein chemical modification and construction of cyclic peptides.-
dc.languageeng-
dc.publisherAcademic Press.-
dc.relation.ispartofChemical Tools for Imaging, Manipulating, and Tracking Biological Systems: Diverse Methods for Optical Imaging and Conjugation-
dc.relation.ispartofseriesMethods in Enzymology ; 639-
dc.subjectProtein bioconjugation-
dc.subjectPeptide cyclization-
dc.subjectBiocompatible reaction-
dc.subjectChemoselective-
dc.subjectOrtho-phthalaldehyde-
dc.titleOrtho-Phthalaldehyde (OPA)-based chemoselective protein bioconjugation and peptide cyclization-
dc.typeBook_Chapter-
dc.identifier.emailZhang, Q: qingz@hku.hk-
dc.identifier.emailLi, X: xuechenl@hku.hk-
dc.identifier.authorityZhang, Q=rp02542-
dc.identifier.authorityLi, X=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/bs.mie.2020.04.016-
dc.identifier.pmid32475404-
dc.identifier.scopuseid_2-s2.0-85085854704-
dc.identifier.hkuros311896-
dc.identifier.spage237-
dc.identifier.epage261-
dc.identifier.isiWOS:000556305400012-
dc.publisher.placeCambridge, MA-
dc.identifier.issnl0076-6879-

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