Chemoselective Peptide Ligation–Desulfurization Chemistry at Aspartate

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Open Access

Field	Value	Language
dc.contributor.author	Thompson, Robert E.
dc.contributor.author	Chan, Bun
dc.contributor.author	Radom, Leo
dc.contributor.author	Jolliffe, Katrina A.
dc.contributor.author	Payne, Richard J.
dc.date.accessioned	2020-06-19
dc.date.available	2020-06-19
dc.date.issued	2013-07-24
dc.identifier.uri	https://hdl.handle.net/2123/22619
dc.description.abstract	Asp‐ecially useful : A synthetic β‐mercapto aspartate residue facilitates the rapid ligation to a range of peptide thioesters. Following the ligation reaction (and without purification), chemoselective desulfurization of the β‐mercapto moiety in the presence of unprotected cysteine residues afforded native peptide products.	en
dc.language.iso	en_US	en
dc.publisher	Wiley	en
dc.relation	ARC DP130101984 and DP1095821	en
dc.rights	Other	en
dc.subject	Aspartate	en
dc.subject	Desulfurization	en
dc.subject	glycopeptide	en
dc.subject	Ligation	en
dc.subject	peptides	en
dc.title	Chemoselective Peptide Ligation–Desulfurization Chemistry at Aspartate	en
dc.type	Article	en
dc.subject.asrc	FoR::030599 - Organic Chemistry not elsewhere classified	en
dc.identifier.doi	10.1002/anie.201304793
dc.type.pubtype	Author accepted manuscript	en
dc.relation.arc	DP130101984
dc.relation.arc	DP1095821
usyd.faculty	SeS faculties schools::Faculty of Science	en