A metallopeptide assembly of the HIV-1 gp41 coiled coil is an ideal receptor in fluorescence detection of ligand binding

A stable fragment of the HIV-1 gp41 inner coiled coil has been designed. The addition of a transition-metal ion to bipyridylated gp41 peptides stabilizes the trimeric helical structure of the coiled coil through the formation of an octahedral tris-bipyridyl complex, and removes nonspecific aggregation of the hydrophobic peptide (see picture). The resulting structure recognizes peptides known to bind to the viral coiled coil and was used to develop a simple, useful and sensitive assay to rapidly detect binding of potential fusion-inhibiting drugs.