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Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study.

ABSTRACT: Binding effect and interaction of N,N'-dialkyl cystine based gemini surfactant (GS); 2(C12Cys) with human serum albumin (HSA) were systematically investigated by the techniques such as surface tension measurement, UV-visible spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking studies. The surface tension measurement exhibited that HSA shifted the critical micelle concentration of the 2(C12Cys) GS to the higher side that confirms the complex formation among 2(C12Cys) GS and HSA which was also verified by UV-visible, fluorescence, and CD spectroscopy. Increase in the concentration of 2(C12Cys) GS increases the absorption of the HSA protein but has a reverse effect on the fluorescence intensity. The analysis of UV-visible study with the help of a static quenching method showed that the value acquired for the bimolecular quenching constant (k q) quenches the intrinsic fluorescence of the HSA protein. Synchronous fluorescence spectrometry declared that the induced-binding conformational changes in HSA and CD results explained the variations in the secondary arrangement of the protein in presence of 2(C12Cys) GS. The present study revealed that the interaction between 2(C12Cys) GS and HSA is important for the preparation and properties of medicines. Molecular docking study provides insight into the specific binding site of 2(C12Cys) GS into the sites of HSA.

SUBMITTER: Aslam J

PROVIDER: S-EPMC6933778 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature

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Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study.

Aslam Jeenat J Lone Irfan Hussain IH Radwan Nagi R E NRE Siddiqui Mohd Faizan MF Parveen Shazia S Alnoman Rua B RB Aslam Ruby R

ACS omega 20191209 26

Binding effect and interaction of N,N'-dialkyl cystine based gemini surfactant (GS); 2(C12Cys) with human serum albumin (HSA) were systematically investigated by the techniques such as surface tension measurement, UV-visible spectroscopy, fluorescence spectroscopy, circular dichroism (CD) spectroscopy, and molecular docking studies. The surface tension measurement exhibited that HSA shifted the critical micelle concentration of the 2(C12Cys) GS to the higher s ...[more]

PMID: 31891097

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Project description:BackgroundBovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.Methodology/principal findingsThe goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (?H) and entropy (?S) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (?G) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the ?-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.Conclusions/significanceIn conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.

Dataset Information

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study.

Publications

Molecular Interaction of Amino Acid-Based Gemini Surfactant with Human Serum Albumin: Tensiometric, Spectroscopic, and Molecular Docking Study.

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