1H NMR studies on the interaction of beta-carboline derivatives with human serum albumin.
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.
Veglia
G
G
Department of Chemistry, University of Rome "La Sapienza", Rome, Italy.
Delfini
M
M
Giudice
M R
MR
Gaggelli
E
E
Valensin
G
G
D002243:Carbolines / Q000737:chemistry* / Q000378:metabolism; D003292:Convulsants / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism
D002243:Carbolines; D003292:Convulsants; D011522:Protons; D012709:Serum Albumin; C036150:beta-carboline-3-carboxylic acid methyl ester