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Peptide ligations accelerated by N-terminal aspartate and glutamate residues.
University of Sydney, Australia.ORCID iD: 0000-0002-0968-5793
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2011 (English)In: Organic Letters, ISSN 1523-7060, E-ISSN 1523-7052, Vol. 13, no 18, p. 4770-3Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2011. Vol. 13, no 18, p. 4770-3
National Category
Organic Chemistry
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URN: urn:nbn:se:kth:diva-211526DOI: 10.1021/ol2017356ISI: 000294703900005PubMedID: 21830797Scopus ID: 2-s2.0-80052771002OAI: oai:DiVA.org:kth-211526DiVA, id: diva2:1129708
Note

QC 20170807

Available from: 2017-08-06 Created: 2017-08-06 Last updated: 2017-08-07Bibliographically approved

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