The study analyzed how nicotine interacts with bovine serum albumin (BSA) using fluorescence and UV-vis spectra, revealing that nicotine causes a regular quenching of BSA's fluorescence.
Quenching mechanisms were identified as dynamic at pH 5.0 and static at pH 7.4 and 11.0, with association constants varying according to temperature and pH levels.
The UV-vis spectra indicated a red shift in BSA's absorbance and a loosening of its secondary structure, suggesting a change from hydrophobic to hydrophilic environments for certain aromatic amino acids in BSA with increased nicotine concentration.