The interaction of a heterocyclic azo compound with itself and with bovine serum albumin (BSA) is realized by probing the structural modifications in Langmuir (L) monolayers and Langmuir-Blodgett (LB) films. It was found from the pressure-area/molecule isotherms that the elastic, thermodynamic, and hysteretic properties of the pure azo L monolayer were strongly altered due to the variation of temperature and pH of subphase water. In addition to that, the modification of such properties of the azo L monolayer due to mixing with BSA was also studied. The incorporation of BSA within the azo molecular assembly reduced the elasticity of that assembly. Such reduction of in-plane elasticity of the pure azo monolayer can also be achieved by reducing the temperature and pH of subphase water without adding BSA. A reduction in area per molecule of the azo assembly at the air-water interface associated with the conformational change from horizontal to vertical orientation facilitating π-π interaction was observed with increase in temperature and pH of the subphase. Such parameters also affected the interactions between azo and BSA molecules within the azo/BSA binary system. The structures of pure azo and binary films can be determined after they are transferred to hydrophilic and hydrophobic Si surfaces using the LB technique. Their out-of-plane and in-plane structures, as extracted from two complementary surface sensitive techniques, X-ray reflectivity and atomic force microscopy, were found to be strongly dependent on mixing with BSA, subphase pH, temperature, and substrate nature.
© 2022 The Authors. Published by American Chemical Society.