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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

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

Akram Mohd M Lal Hira H Shakya Sonam S Kabir-Ud-Din

ACS omega 20200214 7

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</ ...[more]

PMID: 32118178

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Project description:The present work highlights the effect of urea on solvation dynamics and the rotational relaxation of Coumarin 480 (C-480) in the Stern layer of aqueous micelles of cationic gemini surfactants, 12-4(OH) n -12 (n = 0, 1, 2). UV-visible absorption, steady-state fluorescence and fluorescence anisotropy, time-resolved fluorescence and fluorescence anisotropy, and dynamic light scattering measurements have been carried out for this study. The formation of micelles becomes disfavored in the presence of urea at high concentration. Solvation dynamics is bimodal in nature with fast solvation as a major component. The average solvation time increases, reaches a maximum, and then decreases with increasing concentration of urea because the degree of counterion dissociation also follows the same order with the addition of urea in the micellar solution. With increased degree of counterion dissociation, the extent of clustering of water molecules is increased, resulting in slower solvation process. The -OH group present in the spacer group of gemini surfactant controls the rate of solvation by shielding the water molecules from the probe molecules forming hydrogen bond. The microviscosity of micelles is decreased with increasing concentration of urea, as a result of which the rotational relaxation process becomes faster. In the presence of the -OH group in the spacer group, the microviscosity of micelles is enhanced, resulting in longer rotational relaxation time. Rotational relaxation process is bimodal in nature with the major contribution from the fast component to the fluorescence depolarization. Slow rotational relaxation is mainly due to the lateral diffusion of C-480 molecules along the surface of the micelle. The tumbling motion of the micelle as a whole is much slower than the lateral diffusion of C-480. Wobbling motion of C-480 becomes faster with increasing concentration of urea as a result of decreased microviscosity of micelles. The alignment of C-480 molecules in micelles might change with changing microviscosity.

Dataset Information

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

Publications

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

Similar Datasets

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