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

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