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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Bacterial / chemistry
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Bacterial Proteins / chemical synthesis*
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Bacterial Proteins / chemistry
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Chorismate Mutase / chemical synthesis*
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Chorismate Mutase / chemistry
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Chorismate Mutase / metabolism
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Cystine / analogs & derivatives*
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Cystine / chemistry
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Esters / chemistry
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Molecular Conformation
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Mycobacterium tuberculosis / enzymology
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Organoselenium Compounds / chemistry*
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Peptides / chemistry*
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Selenium Compounds / chemistry
Substances
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Antigens, Bacterial
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Bacterial Proteins
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ESAT-6 protein, Mycobacterium tuberculosis
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Esters
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Organoselenium Compounds
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Peptides
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Selenium Compounds
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selenocystine
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Cystine
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Chorismate Mutase