Multispectroscopic and Computational Analysis Insight into the Interaction of Cationic Diester-Bonded Gemini Surfactants with Serine Protease ?-Chymotrypsin.

ABSTRACT: Accumulation of different protein-surfactant mixtures affords further knowledge about the structure-property interactions of biomacromolecules. They will help design suitable surfactants, which, in turn, can enhance the utilization of protein-surfactant complexes in biotechnologies, cosmetics, and food industry realms. Owing to their adaptable and remarkably notable properties, we are describing herein the interaction of C m -E2O-C m gemini surfactants (m = 12, 14, and 16) with ?-CHT by employing various spectroscopic techniques including with molecular docking and density functional theory (DFT) method. Results have revealed complex formation, unfolding, and a static quenching mechanism in the interaction of gemini surfactants with ?-CHT. The Stern-Volmer constant (K SV), quenching constant (k q), the number of binding sites (n), and binding constant (K b) were interrogated by utilizing the fluorescence quenching method, UV-vis, synchronous, 3-D, and resonance Rayleigh scattering fluorescence studies. The data perceive the ?-CHT-C m -E2O-C m complex formation along with conformational alterations induced in ?-CHT. The contribution of aromatic residues to a nonpolar environment is illustrated by pyrene fluorescence. Fourier transform infrared spectroscopy and circular dichroism outcomes reveal conformational modifications in the secondary structure of ?-CHT with the permutation of gemini surfactants. The computational calculations (molecular docking and DFT) further corroborate the complex formation between ?-CHT and C m -E2O-C m gemini surfactants and the contribution of electrostatic/hydrophobic interaction forces therein.

SUBMITTER: Akram M 

PROVIDER: S-EPMC7045504 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature