title: Conformational features of erythrocyte-bound chloroquine from double-selective 1H NMR relaxation.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Siena, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Gaggelli
authors.forename: N
authors.initials: N
authors.lastname: Gaggelli
authors.forename: A
authors.initials: A
authors.lastname: Maccotta
authors.forename: G
authors.initials: G
authors.lastname: Valensin
mesh_terms: 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
chemical_list: D006859:Hydrogen; D002738:Chloroquine; D017666:Deuterium Oxide