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New Insights into the Toxicity of n ‐Butanol to Trypsin: Spectroscopic and Molecular Docking Descriptions
Author(s) -
Zhang Rui,
Sun Tao,
Liu Chunguang,
Song Wei,
Cao Zhaozhen,
Liu Rutao
Publication year - 2015
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21711
Subject(s) - trypsin , chemistry , tryptophan , butanol , conformational change , fluorescence , docking (animal) , binding site , residue (chemistry) , fluorescence spectroscopy , enzyme , stereochemistry , biochemistry , amino acid , ethanol , medicine , physics , nursing , quantum mechanics
n ‐Butanol has been widely used and its residue exists extensively in the environment. It could lead to conformational and functional changes of trypsin by forming a complex with it. Docking method and spectrographic technique were employed to the study of the complex of trypsin and n ‐butanol. The fluorescence results indicated that n ‐butanol can form a complex with trypsin and change the distance between tryptophan and fluorescence quenchers. The conformational changes of trypsin were proved by UV–visible absorption and synchronous fluorescence spectroscopy indicating that n ‐butanol had little effect on the conformation of trypsin at a low concentration while denatured and coagulated the trypsin at a high concentration. The binding site was displayed by molecular modeling, which gave information about distances and binding forces between n ‐butanol and trypsin. The results were in accordance with spectroscopic experiments. Besides, enzyme activity assay gave the dose‐response relationship of n ‐butanol with trypsin.