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A Metallopeptide Assembly of the HIV‐1 gp41 Coiled Coil Is an Ideal Receptor in Fluorescence Detection of Ligand Binding
Author(s) -
Gochin Miriam,
Kiplin Guy Rodney,
Case Martin A.
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352006
Subject(s) - coiled coil , gp41 , chemistry , biophysics , fluorescence , peptide , ligand (biochemistry) , conformational change , crystallography , receptor , stereochemistry , biochemistry , biology , epitope , physics , quantum mechanics , antigen , genetics
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.