Phenytoin-Bovine Serum Albumin interactions - modeling plasma protein - drug binding: A multi-spectroscopy and in silico-based correlation

The graphical abstract serves to highlight the hitherto unreported bathochromic and hypsochromic shifts with respect to BSA and phenytoin respectively. For the first time, the interaction was substantiated by the fluorescence data. Also, we report, for the first time, FT-IR data with regards to the type of bonds formed between Phenytoin and BSA (comparative FT-IR-based analysis). Last but not least, we report, for the first time, LIGPLOT data demonstrating a preponderance and commonality in terms of certain hydrophobic interactions and covalent bonds (two most important interactions relevant to certain Pharmacodynamic variables).100