The role of molecular conformation in ion capture by carboxylic ionophores: a circular dichroism study of narasin A in single-phase solvents and liposomes.
Conformational and thermodynamic aspects of cation binding by the carboxylic ionophore narasin A were studied by circular dichroism (CD). In single-phase solvents, dramatic increases in the maximum differential absorption (delta epsilon) of the C-11 carbonyl were observed upon the binding of K+, Na+ and protons to the free anionic form. These changes were associated with major shifts in the conformation equilibrium between extended and pseudocyclic conformers of narasin. Similar CD changes observed upon the binding of K+ to narasin A in dimyristoylphosphatidylcholine vesicles provided evidence that in the membrane environment, comparable conformation changes were associated with ion binding. Variation of the polar and protic properties of single-phase solvents was also found to influence the delta epsilon of the cation bound species of narasin A, supporting previous evidence for polarity-mediated modulation of conformation. Comparison of cation binding affinities indicated that in both single-phase solvents and liposomes, narasin had a marked equilibrium selectivity for K+ over Na+.
D002412:Cations; D002942:Circular Dichroism; D004134:Dimyristoylphosphatidylcholine; D008081:Liposomes; D008968:Molecular Conformation; D011188:Potassium / Q000378:metabolism*; D011522:Protons; D011714:Pyrans / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism*; D012997:Solvents
D002412:Cations; D008081:Liposomes; D011522:Protons; D011714:Pyrans; D012997:Solvents; D012964:Sodium; C013612:narasin; D011188:Potassium; D004134:Dimyristoylphosphatidylcholine