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Vol. 37 No. 10 (2025): Vol 37 Issue 10, 2025

Copyright (c) 2025 Dr.SUBRAMANI A

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This work is licensed under a Creative Commons Attribution 4.0 International License.

Photophysical and Spectroscopic Insights into the Interaction Mechanism of Azo-Ester Dye with Ovalbumin: A Molecular Docking Perspective

https://doi.org/10.14233/ajchem.2025.34438
A. Gopalakrishnan
PG and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0009-0006-4087-7271
B. Sudharsan
PG and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0009-0001-7313-9068
P. Rajalakshmi
PG and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0009-0005-8893-5058
R. Kumaran
PG and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0000-0002-5358-4447
M. Vanjinathan
PG and Research Department of Chemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0000-0003-4823-2751
A. Subramani
PG and Research Department of Biochemistry, Dwaraka Doss Goverdhan Doss Vaishnav College, Chennai-600106, India
https://orcid.org/0000-0002-0851-268X

Corresponding Author(s) : A. Subramani

subramani@dgvaishnavcollege.edu.in

Asian Journal of Chemistry, Vol. 37 No. 10 (2025): Vol 37 Issue 10, 2025

Abstract

In this work, an azo-ester dye with phenol blocked isocyante and N,N'-dialkanol groups at the ends were studied as fluorescent probe for protein detection. The photophysical properties of the azo-ester dye were characterized both in its unbound state and in the presence of a globular protein like ovalbumin. Upon increasing concentrations of ovalbumin, a significant enhancement in fluorescence intensity was observed, indicating strong interaction between the dye and the protein. The formation of a 1:1 host-guest complex was further supported by competitive binding experiments using hydrogen-bonding molecules such as urea and guanidine hydrochloride (GuHCl), which disrupted the dye-protein complex and led to the formation of solute-protein hydrogen-bonded interactions instead. Molecular docking studies provided the additional insight into the binding mechanism, revealing a negative docking score for the dye-ovalbumin complex, attributed to hydrogen bonding, π–π stacking and multiple hydrophobic interactions. These findings suggest that the dye binds strongly to ovalbumin and may play a role in modulating its activity, highlighting potential applications in therapeutic strategies and cancer prevention.

Keywords

Ovalbumin Fluorescent probe Protein detection Photophysical properties Fluorescence Host-guest complex
(1)
Gopalakrishnan, A.; Sudharsan, B.; Rajalakshmi, P.; Kumaran, R.; Vanjinathan, M.; Subramani, A. Photophysical and Spectroscopic Insights into the Interaction Mechanism of Azo-Ester Dye With Ovalbumin: A Molecular Docking Perspective. ajc 2025, 37, 2561-2570.
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