Premium
Binding of bioactive phytochemical piperine with human serum albumin: A spectrofluorometric study
Author(s) -
Suresh Dodda Venkatanna,
Mahesha Honsigere G.,
Rao A. G. Appu,
Srinivasan Krishnapura
Publication year - 2007
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20735
Subject(s) - piperine , chemistry , binding constant , human serum albumin , fluorescence , tryptophan , chromatography , stereochemistry , binding site , organic chemistry , biochemistry , physics , quantum mechanics , amino acid
Piperine, the bioactive alkaloid compound of the spice black pepper ( Piper nigrum ) exhibits a wide range of beneficial physiological and pharmacological activities. Being essentially water‐insoluble, piperine is presumed to be assisted by serum albumin for its transport in blood. In this study, the binding of piperine to serum albumin was examined by employing steady state and time resolved fluorescence techniques. Binding constant for the interaction of piperine with human serum albumin, which was invariant with temperature in the range of 17–47°C, was found to be 0.5 × 10 5 M −1 , having stoichiometry of 1:1. At 27°C, the van't Hoff enthalpy ΔH° was zero; ΔS° and ΔG° were found to be 21.4 cal mol −1 K −1 and −6.42 kcal mol −1 . The binding constant increased with the increase of ionic strength from 0.1 to 1.0 M of sodium chloride. The decrease of Stern–Volmer constant with increase of temperature suggested that the fluorescence quenching is static. Piperine fluorescence showed a blue shift upon binding to serum albumin, which reverted with the addition of ligands —triiodobenzoic acid and hemin. The distance between piperine and tryptophan after binding was found to be 2.79 nm by Förster type resonance energy transfer calculations. The steady state and time resolved fluorescence measurements suggest the binding of piperine to the subdomain IB of serum albumin. These observations are significant in understanding the transport of piperine in blood under physiological conditions. © 2007 Wiley Periodicals, Inc. Biopolymers 86: 265–275, 2007. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com