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.
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Titolo: | H-1 NMR studies on the interaction of beta-carboline derivatives with human serum albumin | |
Autori: | ||
Data di pubblicazione: | 1998 | |
Rivista: | ||
Citazione: | 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. | |
Handle: | http://hdl.handle.net/11573/15563 | |
Appartiene alla tipologia: | 01a Articolo in rivista |