Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Thomas, GL; Hsieh, YSY; Chun, CKY; Cai, ZL; Reimers, JR; Payne, RJ

Peptide ligations accelerated by N-terminal aspartate and glutamate residues

Thomas, GL Hsieh, YSY Chun, CKY Cai, ZL Reimers, JR

Payne, RJ

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Publication Type:: Journal Article
Citation:: Organic Letters, 2011, 13 (18), pp. 4770 - 4773
Issue Date:: 2011-09-16

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Field	Value	Language
dc.contributor.author	Thomas, GL	en_US
dc.contributor.author	Hsieh, YSY	en_US
dc.contributor.author	Chun, CKY	en_US
dc.contributor.author	Cai, ZL	en_US
dc.contributor.author	Reimers, JR https://orcid.org/0000-0001-5157-7422	en_US
dc.contributor.author	Payne, RJ	en_US
dc.date.issued	2011-09-16	en_US
dc.identifier.citation	Organic Letters, 2011, 13 (18), pp. 4770 - 4773	en_US
dc.identifier.issn	1523-7060	en_US
dc.identifier.uri	http://hdl.handle.net/10453/28184
dc.description.abstract	A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated. © 2011 American Chemical Society.	en_US
dc.relation.ispartof	Organic Letters	en_US
dc.relation.isbasedon	10.1021/ol2017356	en_US
dc.subject.classification	Organic Chemistry	en_US
dc.subject.mesh	Venoms	en_US
dc.subject.mesh	Esters	en_US
dc.subject.mesh	Sulfhydryl Compounds	en_US
dc.subject.mesh	Aspartic Acid	en_US
dc.subject.mesh	Glutamic Acid	en_US
dc.subject.mesh	Peptides	en_US
dc.subject.mesh	Hypoglycemic Agents	en_US
dc.subject.mesh	Molecular Structure	en_US
dc.subject.mesh	Catalysis	en_US
dc.subject.mesh	Stereoisomerism	en_US
dc.subject.mesh	Exenatide	en_US
dc.title	Peptide ligations accelerated by N-terminal aspartate and glutamate residues	en_US
dc.type	Journal Article
utslib.citation.volume	18	en_US
utslib.citation.volume	13	en_US
utslib.for	0306 Physical Chemistry (incl. Structural)	en_US
utslib.for	03 Chemical Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Mathematical and Physical Sciences
utslib.copyright.status	closed_access
pubs.issue	18	en_US
pubs.publication-status	Published	en_US
pubs.volume	13	en_US

Abstract:

A novel application of intramolecular base catalysis confers enhanced reaction rates for aminolysis ligations between peptide thioesters and peptides bearing N-terminal aspartate or glutamate residues. The broad scope of this process and its application in the total synthesis of the diabetes drug exenatide is demonstrated. © 2011 American Chemical Society.

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http://hdl.handle.net/10453/28184