Conformational features of erythrocyte-bound chloroquine from double-selective 1H NMR relaxation.
The interaction between the antimalarial drug chloroquine and red blood cells was investigated by measuring 1H NMR spin-lattice relaxation rates upon double-selective excitation of dipolarly connected spin pairs within the ligand molecule. Geometric and dynamic features were inferred, for the free as well as for the bound ligand, by the cross-relaxation terms between protons at fixed and time-dependent distances, respectively. A change in orientation of the side chain in respect of the aromatic moiety was shown to result from the binding interaction.
Gaggelli
E
E
Department of Chemistry, University of Siena, Italy.
Gaggelli
N
N
Maccotta
A
A
Valensin
G
G
D002738:Chloroquine / Q000097:blood* / Q000737:chemistry*; D017666:Deuterium Oxide; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008968:Molecular Conformation; D015394:Molecular Structure
D006859:Hydrogen; D002738:Chloroquine; D017666:Deuterium Oxide