Interactions of AsCy3 with Cysteine-Rich Peptides | Zendy

Seth C. Alexander | Zendy; Alanna Schepartz | Zendy

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Interactions of AsCy3 with Cysteine-Rich Peptides

Author(s) -

Seth C. Alexander,

Alanna Schepartz

Publication year - 2014

Publication title -

organic letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.94

H-Index - 239

eISSN - 1523-7060

pISSN - 1523-7052

DOI - 10.1021/ol501721j

Subject(s) - chemistry , cysteine , biomolecule , fluorescence , amino acid , ligand (biochemistry) , combinatorial chemistry , peptide , stereochemistry , biochemistry , receptor , enzyme , physics , quantum mechanics

There is great interest in fluorogenic compounds that tag biomolecules within cells. Biarsenicals are fluorogenic compounds that become fluorescent upon binding four proximal Cys thiols, a tetracysteine (Cys(4)) motif. This work details interactions between the biarsenical AsCy3 and Cys(4) peptides. Maximal affinity was observed when two Cys-Cys pairs were separated by at least 8 amino acids; the highest affinity ligand bound in the nanomolar concentration range (K(app) = 43 nM) and with a significant (3.2-fold) fluorescence enhancement.

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