The conformation of cytochalasin D in DMSO solution from 1H and 13C NMR relaxation rates

Abstract

The conformation of cytochalasin D in solution has been delineated by measuring ¹³C and ¹H NMR spin–lattice relaxation rates and NOESY spectra. The motional correlation time was evaluated at 0.26 ns at 300 K. A comparison with the structure of cytochalasin B in the same solvent discloses several similarities, except for a small distortion of the five-membered ring. The difference in activity is therefore ascribed to the different hydrophobicity of substituents within the macrocycle.