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

Gianluigi Veglia, Maurizio Delfini, Maria Rosaria Del Giudice, Elena Gaggelli, Gianni Valensin

Research output: Contribution to journalArticle

24 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)281-286
Number of pages6
JournalJournal of Magnetic Resonance
Volume130
Issue number2
DOIs
StatePublished - Feb 1998

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