Rapid additive-free selenocystine-selenoester peptide ligation.

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

Journal: Journal of the American Chemical Society 2016;137(44):14011-4

PMID: 26487084

Full Text on American Chemical Society View on PubMed

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.

Address: School of Chemistry, The University of Sydney , Sydney, NSW 2006, Australia.

DOI: 10.1021/jacs.5b07237

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https://doi.org/10.1021/jacs.5b07237

MeSH Terms: Antigens, Bacterial, Bacterial Proteins, Chorismate Mutase, Cystine, Esters, Molecular Conformation, Mycobacterium tuberculosis, Organoselenium Compounds, Peptides, Selenium Compounds