Probing the interaction between selected furan derivatives and porcine myofibrillar proteins by spectroscopic and molecular docking approaches.

The interactions between myofibrillar proteins (MPs) and furan derivatives were researched by spectroscopic and molecular docking approaches. The gas chromatography-mass spectrometry results showed that the binding capacity of MPs to the furan derivatives decreased in the order 5-methyl furfural > furfural > 2-acetylfuran > furfuryl alcohol. It largely depended on molecular polarity and the position of the branched chain of the furan derivatives. Fluorescence analysis showed that the interaction between furan derivatives and MPs was a combination of static and dynamic quenching, affecting the tryptophan and tyrosine residue microenvironment of MPs. After the interaction, the conformational investigation showed that the presence of furan derivatives decreased the contents of ordered structures of MPs, transforming them into random coils. According to the molecular docking model and thermodynamic parameters, hydrogen bonds, van der Waals forces and hydrophobic interactions were considered to be the main interaction forces between MPs and all four furan derivatives.