Rapid Additive-Free Selenocystine–Selenoester Peptide Ligation

Mitchell, Nicholas J.; Malins, Lara R.; Liu, Xuyu; Thompson, Robert E.; Chan, Bun; Radom, Leo; Payne, Richard J.

Access status:

Open Access

Field	Value	Language
dc.contributor.author	Mitchell, Nicholas J.
dc.contributor.author	Malins, Lara R.
dc.contributor.author	Liu, Xuyu
dc.contributor.author	Thompson, Robert E.
dc.contributor.author	Chan, Bun
dc.contributor.author	Radom, Leo
dc.contributor.author	Payne, Richard J.
dc.date.accessioned	2020-05-12
dc.date.available	2020-05-12
dc.date.issued	2015-10-21
dc.identifier.citation	Nicholas J. Mitchell, Lara R. Malins, Xuyu Liu, Robert E. Thompson, Bun Chan, Leo Radom, and Richard J. Payne Journal of the American Chemical Society 2015 137 (44), 14011-14014 DOI: 10.1021/jacs.5b07237	en_AU
dc.identifier.uri	https://pubs.acs.org/doi/10.1021/jacs.5b07237
dc.identifier.uri	https://hdl.handle.net/2123/22285
dc.description.abstract	We describe an unprecedented reaction between peptide selenoesters and peptide dimers bearing N-terminal selenocystine that proceeds in aqueous buffer to afford native amide bonds without the use of additives. The selenocystine-selenoester ligations are complete in minutes, even at sterically hindered junctions, and can be used in concert with one-pot deselenization chemistry. Various pathways for the transformation are proposed and probed through a combination of experimental and computational studies. Our new reaction manifold is also showcased in the total synthesis of two proteins.	en_AU
dc.language.iso	en_US	en_AU
dc.publisher	American Chemical Society	en_AU
dc.relation	ARC FT130150100	en_AU
dc.subject	Peptides and proteins	en_AU
dc.subject	Monomers	en_AU
dc.subject	Oligomers	en_AU
dc.subject	Ligation Acyls	en_AU
dc.title	Rapid Additive-Free Selenocystine–Selenoester Peptide Ligation	en_AU
dc.type	Article	en_AU
dc.subject.asrc	FoR::030599 - Organic Chemistry not elsewhere classified	en_AU
dc.identifier.doi	10.1021/jacs.5b07237
dc.type.pubtype	Post-print	en_AU