H NMR Studies on the Interaction of β-Carboline Derivatives with Human Serum Albumin |
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Authors: | Gianluigi Veglia Maurizio Delfini Maria Rosaria Del Giudice Elena Gaggelli Gianni Valensin |
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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 |
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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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