Physicochemical Properties of a Bi-aromatic Heterocyclic-Azo/BSA Hybrid System at the Air-Water Interface.

ABSTRACT: 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

SUBMITTER: Bal JK 

PROVIDER: S-EPMC9089336 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature