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Chemically Diverse Helix-Constrained Peptides Using Selenocysteine Crosslinking.

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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… Click to show full abstract

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.

Keywords: using selenocysteine; chemically diverse; diverse helix; helix constrained; constrained peptides; peptides using

Journal Title: Organic letters
Year Published: 2018

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