Background: Ferulic acid (FA), a phenolic acid widely occurring in nature, has attracted extensive attention because of its biological activity. Ovalbumin (OVA) is a commonly used carrier protein. The mechanism of FA binding with OVA was investigated by utilizing a variety of spectral analyses, accompanied by computer simulation.
Results: It was discovered that the fluorescence quenching mechanism of OVA by FA was a static mode as a result of the formation of an FA-OVA complex, which was verified by the concentration distributions and pure spectrum of the constituents decomposed from the high overlap spectrum signals using multivariate curve resolution-alternate least squares algorithm. Hydrogen bonds and Van der Waals forces drove the formation of FA-OVA complex with a binding constant of 1.69 × 104 L mol-1 . The presence of FA induced the loose structure of OVA with an attenuation of α-helix content and improved the thermal stability of OVA. Computer docking indicated that FA interacted with the amino acid residues Arg84, Asn88, Leu101 and Ser103 of OVA through hydrogen bonds. Molecular dynamics simulation proved that the combination of FA with OVA boosted the conformational stability of OVA and hydrogen bonds brought a crucial part in stabilizing the structure of the complex.
Conclusions: The study may supply the theoretical basis for the design of FA transport system using OVA as carrier protein to improve the instability and low bioavailability of FA. © 2021 Society of Chemical Industry.
Keywords: binding characteristic; ferulic acid; molecular dynamics simulation; ovalbumin.
© 2021 Society of Chemical Industry.