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JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking.
Organic Letters 2018 March 3
The use of selenocysteines and various cross-linkers to induce helicity in a bioactive peptide is described. The higher reactivity of selenocysteine, relative to cysteine, facilitates rapid cross-linking within unprotected linear peptides under mild aqueous conditions. Alkylating agents of variable topology and electrophilicity were used to link pairs of selenocysteines within a p53 peptide. Facile selenoether formation enables diverse tailoring of the helical peptide structure.
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