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Spectroscopic identification of interactions of formaldehyde with bovine serum albumin
Author(s) -
Liu Yihong,
Liu Rutao,
Mou Yue,
Zhou Guangjun
Publication year - 2010
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.20364
Subject(s) - formaldehyde , bovine serum albumin , circular dichroism , chemistry , fluorescence , absorption (acoustics) , serum albumin , albumin , biochemistry , biophysics , biology , materials science , physics , quantum mechanics , composite material
The mechanism of formaldehyde–protein interactions was investigated by determining the effects of formaldehyde on the common protein bovine serum albumin (BSA). The effects at the molecular level were determined by fluorescence, ultraviolet absorption, and circular dichroism (CD) spectrometry. Formaldehyde could decrease the amount of alpha‐helix, leading to loosening of the protein skeleton. In the loose structure, internal amino acids are exposed and the characteristic fluorescence of BSA is obviously quenched. The spectroscopic results reveal that formaldehyde exposure induces changes in the microenvironment and conformation of serum albumin, which could lead to toxic effects on the organism. © 2010 Wiley Periodicals, Inc. J Biochem Mol Toxicol 25:95–100, 2011; View this article online at wileyonlinelibrary.com . DOI 10.1002/jbt.20364