1H NMR Studies on the Interaction of β-Carboline Derivatives with Human Serum Albumin

✍ Scribed by Gianluigi Veglia; Maurizio Delfini; Maria Rosaria Del Giudice; Elena Gaggelli; Gianni Valensin

• Publisher: Elsevier Science
• Year: 1998
• Tongue: English
• Weight: 157 KB
• Volume: 130
• Category: Article
• ISSN: 1090-7807
• DOI: 10.1006/jmre.1997.1301

✦ Synopsis

1H 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.