Effect of triazole‐tryptophan hybrid on the conformation stability of bovine serum albumin |
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| Authors: | Amir Azam Amit Kumar Mohammad Abid Rajan Patel |
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| Affiliation: | 1. Department of Chemistr, Jamia Millia Islamia, New Delhi, India;2. Centre for Nano and Material Sciences, Jain University, Bangalore, India;3. Medicinal Chemistry Laboratory, Department of Biosciences, Jamia Millia Islamia, New Delhi, India;4. Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi, India |
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| Abstract: | The effect of a potent antimicrobial compound bearing 1,2,3‐triazole core and a tryptophan tail, triazole‐tryptophan hybrid (TTH), with bovine serum albumin (BSA) have been explored using various spectroscopic and molecular docking methods. Studies revealed that TTH strongly quenches the intrinsic fluorophore of BSA by a static quenching mechanism. Time‐resolved fluorescence spectra further confirmed the involvement of static quenching for TTH–BSA system. The calculated thermodynamic parameters; ΔH, ΔS, and ΔG showed that the binding process was spontaneous, exothermic and entropy driven. Synchronous fluorescence, three‐dimensional (3D) fluorescence and circular dichroism data revealed that TTH induces the structural alteration in BSA and enhances its stability. In silico study of TTH–BSA system showed that it binds with BSA at the site I of subdomain IIA. Both the experimental and in silico study showed that the hydrophobic and electrostatic interactions play a major role in TTH–BSA binding. |
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| Keywords: | bovine serum albumin fluorescence molecular docking time resolved triazole‐tryptophan hybrid UV‐visible |
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