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.
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