H-1 NMR studies were performed on two beta-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 beta-carboline moiety was shown to yield lower association constants, slower dissociation rates, and diverse interacting modes with the indole hydrophobic site of the protein. (C) 1998 Academic Press.
H-1 NMR studies on the interaction of beta-carboline derivatives with human serum albumin / G., Veglia; Delfini, Maurizio; M. R., Del Giudice; E., Gaggelli; G., Valensin. - In: JOURNAL OF MAGNETIC RESONANCE. - ISSN 1090-7807. - 130:2(1998), pp. 281-286. [10.1006/jmre.1997.1301]
H-1 NMR studies on the interaction of beta-carboline derivatives with human serum albumin
DELFINI, Maurizio;
1998
Abstract
H-1 NMR studies were performed on two beta-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 beta-carboline moiety was shown to yield lower association constants, slower dissociation rates, and diverse interacting modes with the indole hydrophobic site of the protein. (C) 1998 Academic Press.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.