Unraveling the interaction of bisphenol A with collagen and its effect on conformational and thermal stability

Evidence suggests the association of bisphenol A (BPA) with increased collagen (COL) expression in the development of fibrosis. Ultraviolet and fluorescence spectra on collagen-BPA interaction showed that 100 ng/ml of BPA initiated loosening of protein backbone through unfolding with exposure of tyrosine residues resulting in an intermediate "Molten Globule" state, which later aggregated with 1 μg/ml of BPA indicated with an apparent red-shift. Conformational changes with CD and ATR-FTIR showed disappearance of negative band with broadening and shifting of peptide carbonyl groups. Light scattering findings with TEM images presented initial dissolution followed by unordered thick fibrillar bundles with 30 μg/ml BPA. The complex was pH sensitive, with calorimetric thermogram revealing increased thermal stability requiring 83°C to denature. Hydrogen bonds of 2.8 Å with hydrophobic interactions of BPA in all grooves of collagen molecule with same pattern and binding energy (-4.1 to -3.9 kcal/mol) confirmed the intensity of aggregate formation via in-silico docking.