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Synthesis and study on the binding of thiazol‐2(3H)‐ylidine derivative with human serum albumin using spectroscopic and molecular docking methods
Author(s) -
Hassan Mohammad Fahimul,
Rauf Abdul
Publication year - 2017
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.3227
Subject(s) - human serum albumin , chemistry , quenching (fluorescence) , tryptophan , hydrogen bond , circular dichroism , fluorescence , förster resonance energy transfer , docking (animal) , fourier transform infrared spectroscopy , fluorescence spectroscopy , hydrophobic effect , conformational change , photochemistry , crystallography , stereochemistry , molecule , organic chemistry , chromatography , amino acid , biochemistry , medicine , physics , nursing , quantum mechanics
Abstract In this article, a facile and convenient synthesis of thiazol‐2(3H)‐ylidine derivatives of fatty acid ( 3a – c ) is described. The binding of N ′‐(4,5‐dimethyl‐3‐penylthiazol‐2(3H)‐ylidine)octadec‐9‐enehydrazide ( 3a ) with human serum albumin (HSA) is explored using various spectral methods and molecular docking. Fluorescence quenching results show that 3a induces conformational changes in HSA and the polarity around the tryptophan residues is increased. Stern–Volmer quenching plots at different temperatures (298, 305 and 312 K) show that the fluorescence quenching mechanism is static quenching. Synchronous fluorescence, 3D fluorescence spectra, circular dichroism and Fourier transform infrared spectroscopy are used to determine the structural change in HSA on interaction with 3a . Förster resonance energy transfer analysis shows that the binding distance ( r 0 = 2.78 nm) between HSA (Trp214) and 3a is within the of range 2–8 nm for quenching to occur. The molecular docking study also confirms that 3a is located in subdomain IIA (site I) of HSA and is stabilized by hydrogen bonding and hydrophobic forces.