Interaction between the antioxidant compound safranal and α-chymotrypsin in spectroscopic fields and molecular modeling approaches

• Published in: Journal of biomolecular structure & dynamics Vol. 42; no. 8; pp. 4097 - 4109
• Main Authors: Zohreh Vahedi, Seyedeh, Farhadian, Sadegh, Shareghi, Behzad, Asgharzadeh, Sanaz
• Format: Journal Article
• Language: English
• Published: England Taylor & Francis 23.05.2024
• Subjects: Antioxidants - chemistry; Antioxidants - metabolism; Chymotrypsin - chemistry; Chymotrypsin - metabolism; Crocus - chemistry; Cyclohexenes - chemistry; Cyclohexenes - metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; kinetic; Models, Molecular; Molecular Docking Simulation; Molecular Dynamics Simulation; Protein Binding; safranal; simulation; spectroscopy; Terpenes - chemistry; Terpenes - metabolism; Thermodynamics; α-Chy; α-Chy; safranal; kinetic; spectroscopy; simulation
• ISSN: 0739-1102; 1538-0254; 1538-0254
• DOI: 10.1080/07391102.2023.2272186

Among various herbal plants, saffron has been the subject of study in various medical and food fields. Among the compounds of saffron, safranal is one of them. Safranal is a monoterpene aldehyde. The precursor of safranal is called picrocrocin, whose hydrolysis leads to the production of safranal. picrocrocin has two sugar components and aglycone. sugar component was separated during the drying process of saffron and safranal is produced. Saffron is the cause of the saffron aroma. Previous studies have shown that safranal offers many benefits such as antioxidants, blood pressure regulation and anti-tumor qualities. On the other hand, α-Chy is an enzyme secreted by the pancreas into the intestine and then acts as an efficient protease. In this study, various methods, such as molecular dynamics (MD) simulation and molecular binding, and different spectroscopic techniques, as well as protein stability techniques, were used to investigate the possible interactions between safranal and α-Chy. UV spectroscopic studies were showing that the existence of safranal decreased α-Chy absorption intensity. safranal caused the intrinsic fluorescence of α-Chy to be quenched too. According to the Stern-Volmer equation, the interaction between safranal and α-Chy was of the static type. In thermodynamic calculations, the interaction between safranal and α-Chy was stabilized by hydrophobic forces. And it was found that this interaction continued spontaneously. These results were, thus, consistent with the Docking data simulation (with the negative ΔG° number and positive changes in enthalpy and entropy). The thermal stability of α-Chy was also measured, showing that its melting point was shifted to a higher threshold as a result of the interaction. also, MD simulation indicated that α-Chy became more stable in the presence of safranal. In this paper, all the results of the laboratory techniques were confirmed by molecular dynamic simulations, so the correctness of the results was confirmed. From this research, we hope to carefully observe the possible changes in the behavior and structure of the enzyme in the presence of safranal. Communicated by Ramaswamy H. Sarma