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Effect of pH on Diclofenac-Lysozyme Interaction: Structural and Functional Aspect
Mohd Basheeruddin1, Sheeza Khan1, Neesar Ahmed1
1School of Life Sciences, B. S. Abdur Rahman Crescent Institute of Science and Technology, Chennai, India.
Diclofenac (DCF) destabilizes lysozyme structure and function. This nonsteroidal anti-inflammatory drug
Area of Science:
- Biochemistry
- Pharmacology
Background:
- Diclofenac (DCF) is a nonsteroidal anti-inflammatory drug (NSAID) with known side effects.
- Long-term NSAID use can lead to cardiovascular and renal complications.
Purpose of the Study:
- To investigate the impact of diclofenac on the structural integrity, stability, and function of lysozyme.
- To analyze diclofenac's effects across various pH conditions.
Main Methods:
- Heat-induced denaturation of lysozyme was monitored.
- Thermodynamic parameters (Tm, ΔHm, ΔCp, ΔGDo) were determined in the presence and absence of varying diclofenac concentrations at different pH values.
Main Results:
- Diclofenac destabilized lysozyme, indicated by changes in Tm and ΔGDo across all tested pH values.
- Protein destabilization was less pronounced at acidic pH (2.0) compared to physiological pH (7.0).
- Structural changes were less significant at pH 2.0 than pH 7.0, with quenching observed at both pH values.
Conclusions:
- Diclofenac negatively affects lysozyme stability and structure.
- The destabilizing effect of diclofenac on lysozyme is entropically driven.
- Understanding these interactions is crucial for evaluating NSAID safety and potential therapeutic applications.
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