Shifting the equilibrium mixture of gramicidin double helices toward a single conformation with multivalent cationic salts.
The conformation of the polypeptide antibiotic gramicidin is greatly influenced by its environment. In methanol, it exists as an equilibrium mixture of four interwound double-helical conformers that differ in their handedness, chain orientation, and alignment. Upon the addition of multivalent cationic salts, there is a shift in the equilibrium to a single conformer, which was monitored in this study by circular dichroism spectroscopy. With increasing concentrations of multivalent cations, both the magnitude of the entire spectrum and the ratio of the 229-nm to the 210-nm peak were increased. The spectral change is not related to the charge on the cation, but appears to be related to the cationic radius, with the maximum change in ellipticity occurring for cations with a radius of approximately 1 A. The effect requires the presence of an anion whose radius is greater than that of a fluoride ion, but is otherwise not a function of anion type. It is postulated that multivalent cations interact with a binding site in one of the conformers, known as species 1 (a left-handed, parallel, no stagger double helix), stabilizing a modified form of this type of structure.
Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, England.
D A
DA
Doyle
B A
BA
Wallace
D000595:Amino Acid Sequence; D001665:Binding Sites; D002412:Cations / Q000737:chemistry*; D002942:Circular Dichroism; D006096:Gramicidin / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012492:Salts; D012997:Solvents
D002412:Cations; D012492:Salts; D012997:Solvents; D006096:Gramicidin