Exploring the binding mechanism of ferulic acid and ovalbumin: insights from spectroscopy, molecular docking and dynamics simulation

Abstract

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 × 10 4 L mol −1 . The presence of FA induced the loose structure of OVA with an attenuation of ⊍-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.

Inhibition of Iron Release from Donkey Spleen Ferritin through Malt-Derived Protein Z–Ferulic Acid Interactions

“…The numbers of hydrogen bonds within 100 ns during MD were recorded in Figure 5C, illustrating that there were 1-3 hydrogen bonds maintained between FA and PZ during the MD process. The results were in accordance with the form research, which had shown 2-3 hydrogen bonds between PZ and curcumin, and 0-4 hydrogen bonds between ovalbumin and FA [25,46]. As one of the main non-covalent interactions, hydrogen bonds play a crucial role in non-covalent interactions of the PZ-FA complex.…”

“…Additionally, the leading contribution of PZ-FA binding is van der Waals energy (−28.88 ± 2.04 kcal/mol), followed by electrostatic energy (−21.30 ± 2.77 kcal/mol), and then the non-polar contribution to solvation (−4.61 ± 0.05 kcal/mol). This result correlated well with the ovalbumin-FA interactions, and its binding free energy reached −26.78 kcal/mol [46]. For further analysis of binding energy, we explored the contribution of amino acids to binding.…”

Screening and Inhibition Mechanism of Xanthine Oxidase Inhibitors in Ethanolic Extracts of Chimonanthus salicifolius Hu Leaves

“…Molecular simulation can directly display the binding mode of small molecule ligands with XO [32] . Figure 7 A and D respectively showed the optimal binding sites of quercetin and kaempferol with XO after 100 times of docking.…”

Shedding light on the interaction of ovalbumin and resveratrol: structure, digestibility, transport, and allergenicity assessment of OVA–RES complexes

“…Molecular docking was performed with the Discovery Studio 3.5 program. 19 The crystal structure of OVA (code 1OVA) was acquired from the RCSB Protein Data Bank (http://www.rcsb.org/ structure/1OVA) and was treated by adding Gasteiger charges and polar hydrogen atoms to obtain the monomer OVA used for molecular docking. Next, the molecular model of RES (Pubchem CID: 445154) was downloaded from the Pubchem website.…”