Exploring interaction dynamics of designed organic cocrystal charge transfer complex of 2-hydroxypyridine and oxalic acid with human serum albumin: Single crystal, spectrophotometric, theoretical and antimicrobial studies.

As human serum albumin (HSA) being the most abundant blood protein involved in the role of transport of molecules (drugs), we have designed HSA binding organic charge transfer complex between 2-hydroxypyridine (donor) and oxalic acid (acceptor) showing antimicrobial activities. The type of interactions between HSA and synthesized complex at the molecular level was studied through fluorescence spectroscopy. Binding constant along with the type of quenching mechanism was shown through the Stern Volmer equation.