Binding affinity and mechanism of dicofol-lysozyme interaction: Insights from multi-spectroscopy and molecular dynamic simulations

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 142569 - 142569

Published: March 1, 2025

Language: Английский

Evaluation of the structure and stability of myoglobin after interaction with ribose: spectroscopic and molecular simulation approach

Journal of Biomolecular Structure and Dynamics, Journal Year: 2025, Volume and Issue: unknown, P. 1 - 12

Published: May 2, 2025

Osmolytes, as small organic molecules, possess a remarkable ability to exert protective effects on biomacromolecules, including proteins, while preserving their inherent functionality. Myoglobin, globular protein comprising sequence of 153 amino acids, fulfills crucial biological role by exhibiting reversible oxygen binding capabilities and facilitating its efficient transfer the muscular tissues. In this study, ribose myoglobin in sodium phosphate buffer were studied UV-Vis's spectrophotometry spectrofluorimetric investigations at pH 7.4. Also, interaction was theoretically through molecular dynamics simulation docking techniques. The results showed that stabilizes structure increasing melting temperature (Tm) myoglobin. fluorescence intensity decreased with static quenching mechanism different temperatures. thermodynamic data obtained from experimental also predicted intermolecular forces affecting formation myoglobin-ribose complex are mainly van der Waals interactions hydrogen bindings. Theoretical analyses unveiled favored site within Subsequent simulations validated stability formed between Our findings fundamental for understanding molecular-level details myoglobin-ligand interactions, opening avenues innovative approaches prevent or alleviate dysfunction various disease conditions.

Language: Английский

Evaluation of the effects of amitraz on the enzyme activity and stability of lysozyme: Spectroscopic and MD simulation approach

Chemosphere, Journal Year: 2024, Volume and Issue: 370, P. 144004 - 144004

Published: Dec. 28, 2024

Language: Английский