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H NMR Studies on the Interaction of β-Carboline Derivatives with Human Serum Albumin
Authors:Gianluigi Veglia  Maurizio Delfini  Maria Rosaria Del Giudice  Elena Gaggelli  Gianni Valensin
Affiliation:aDepartment of Chemistry, University of Rome “La Sapienza” Rome, Italy;bLaboratorio di Chimica del Farmaco, Istituto Superiore di Sanità, Rome, Italy;cDepartment of Chemistry, University of Siena, Pian dei Mantellini 44, Siena, 53100, Italy
Abstract:1H NMR studies were performed on two β-carboline derivatives interacting with human serum albumin. The spin–lattice relaxation rates of the two derivatives, having side chains of different length and polarity, were used to demonstrate a diverse motional behavior in solution together with slightly different relaxation pathways. Single- and double-selective excitation made it possible to evaluate dynamics in the free and protein-bound states. Occurrence of a relatively long hydrophilic chain interacting with the proton-acceptor nitrogen of the β-carboline moiety was shown to yield lower association constants, slower dissociation rates, and diverse interacting modes with the indole hydrophobic site of the protein.
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