Elucidating the significance of molecular interaction between sulphur doped zinc oxide nanoparticles and serum albumin using multispectroscopic approach

Mahanthappa, M and Savanur, MA and Ramu, J and Tatagar, A (2023) Elucidating the significance of molecular interaction between sulphur doped zinc oxide nanoparticles and serum albumin using multispectroscopic approach. In: Journal of Molecular Recognition, 36 (11).

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Abstract

Ingenious nanomaterials with improved biocompatibility and multifunctional properties are gaining vital significance in biomedical applications, including advanced drug delivery and nanotheranostics. In a biological system, these nanoparticles interact with serum proteins forming a dynamic corona that affects their biological or toxicological properties producing undesirable effects. Thus, the current study focuses on the synthesis of sulphur-doped zinc oxide nanoparticles (ZnO/S NPs) and characterizing their mechanism of interaction with serum proteins using multispectroscopic approach. ZnO/S NPs were synthesized by employing a co-precipitation approach and characterized using various analytical techniques. The results of interaction studies demonstrated that ZnO/S NPs interact with serum albumins via the static quenching process. Analysis of thermodynamic parameters (ΔG, ΔH and ΔS) revealed that the binding process is spontaneous, exothermic and van der Waals force or hydrogen bonding plays a major role. The interaction of ZnO/S NPs with tyrosine residue in bovine serum albumin was established by synchronous fluorescence spectroscopy. In addition, the results of UV–visible, circular dichroism, Fourier transform infrared, Forster's resonance energy transfer theory and dynamic light scattering spectroscopic studies revealed that the ZnO/S NPs interact with albumin by inducing the conformational changes in secondary structure and reducing the α-helix content. © 2023 John Wiley & Sons Ltd.

Item Type:	Journal Article
Publication:	Journal of Molecular Recognition
Publisher:	John Wiley and Sons Ltd
Additional Information:	The copyright for this article belongs to the John Wiley and Sons Ltd.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	24 Nov 2023 10:50
Last Modified:	24 Nov 2023 10:50
URI:	https://eprints.iisc.ac.in/id/eprint/83218

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