1H NMR Studies on the Interaction of β-Carboline Derivatives with Human Serum Albumin
Source: Journal of Magnetic Resonance, Volume 130, Number 2, February 1998 , pp. 281-286(6)
Publisher: Academic Press
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.
Document Type: Research Article
Affiliations: 1: Department of Chemistry, University of Rome “La Sapienza”, Rome, Italy 2: Laboratorio di Chimica del Farmaco, Istituto Superiore di Sanità, Rome, Italy 3: Department of Chemistry, University of Siena, Pian dei Mantellini 44, Siena, 53100, Italy
Publication date: February 1, 1998