Fluorescence monitoring of binding of a Zn (II) complex of a Schiff base with human serum albumin

• Published in: International journal of biological macromolecules Vol. 226; pp. 1515 - 1522
• Main Authors: Sahoo, Dipak Kumar, Dasgupta, Souradip, Kistwal, Tanuja, Datta, Anindya
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 31-01-2023
• Subjects: Binding Sites; Circular Dichroism; FCS; FRET; Human serum albumin; Humans; Molecular docking; Molecular Docking Simulation; Protein Binding; Schiff Bases - chemistry; Serum Albumin, Human - chemistry; Spectrometry, Fluorescence - methods; TCSPC; Thermodynamics; Warfarin; Zinc - chemistry; TCSPC; Human serum albumin; Warfarin; FRET; Molecular docking; FCS
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2022.11.263

Zn (II) complexes of Schiff bases have potential applications in biomedical sciences as imaging agents, cancer therapeutics and diagnostics. Thus, it is important to understand their interaction with carrier proteins, like serum albumins. The present paper focuses on the binding interactions between Human serum albumin (HSA) and Znsalampy, making use of fluorescence spectroscopic techniques at ensemble as well as at single molecular level. An idea about the binding constant is obtained from the quenching of the single Trp (Tryptophan) residue of HSA by Znsalampy. Fluorescence correlation spectroscopy (FCS) has also been used to monitor the protein-ligand binding. The location of Znsalampy in its complex with HSA is determined by competitive binding experiments and molecular docking calculations. The binding constant obtained from the Znsalampy-HSA interaction falls in the ideal range for biological applications and the location is found to be in the proximity of Sudlow's site I. The esterase activity of HSA is retained in the presence of the Znsalampy. Hence, it is concluded that this Znsalampy may be a potential probe and biomarker in biomedical applications.
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