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Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods.

ABSTRACT: The interaction between myofibrillar proteins (MPs) and capsaicin (CAP) was investigated using multispectral, molecular docking, and molecular dynamics simulation methods. The resulting complex increased the hydrophobicity of the tryptophan and tyrosine microenvironment as revealed by fluorescence spectral analysis. The fluorescence burst mechanism study indicated that the fluorescence burst of CAP on the MPs was a static one (Kq = 1.386 × 10¹² m^-1s^-1) and that CAP could bind with MPs well (Ka = 3.31 × 10⁴ L/mol, n = 1.09). The analysis of circular dichroism demonstrated that the interaction between CAP and MPs caused a decrease in the α-helical structure of MPs. The complexes formed exhibited lower particle size and higher absolute ζ potential. Furthermore, hydrogen bonding, van der Waals forces, and hydrophobic interactions were found to be the primary factors facilitating the interaction between CAP and MPs, as suggested by molecular docking models and molecular dynamics simulations.

SUBMITTER: Wu Z

PROVIDER: S-EPMC10314199 | biostudies-literature | 2023 Jun

REPOSITORIES: biostudies-literature

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Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods.

Wu Zhicheng Z Xu Jingbing J Ruan Jinggang J Chen Jiaxin J Li Xue X Yu Yiru Y Xie Xinrui X Tang Jie J Zhang Dong D Li Hongjun H

Food chemistry: X 20230603

The interaction between myofibrillar proteins (MPs) and capsaicin (CAP) was investigated using multispectral, molecular docking, and molecular dynamics simulation methods. The resulting complex increased the hydrophobicity of the tryptophan and tyrosine microenvironment as revealed by fluorescence spectral analysis. The fluorescence burst mechanism study indicated that the fluorescence burst of CAP on the MPs was a static one (Kq = 1.386 × 1012 m-1s-1) and that C ...[more]

PMID: 37397215

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Project description:Transient receptor potential vanilloid subtype 1 (TRPV1) is a heat-sensitive ion channel also involved in pain sensation, and is the receptor for capsaicin, the active ingredient of hot chili peppers. The recent structures of TRPV1 revealed putative ligand density within the S1 to S4 voltage-sensor-like domain of the protein. However, questions remain regarding the dynamic role of the lipid bilayer in ligand binding to TRPV1. Molecular dynamics simulations were used to explore behavior of capsaicin in a 1-palmitoyl-2-oleoyl phosphatidylcholine bilayer and with the target S1-S4 transmembrane helices of TRPV1. Equilibrium simulations reveal a preferred interfacial localization for capsaicin. We also observed a capsaicin molecule flipping from the extracellular to the intracellular leaflet, and subsequently able to access the intracellular TRPV1 binding site. Calculation of the potential of mean force (i.e., free energy profile) of capsaicin along the bilayer normal confirms that it prefers an interfacial localization. The free energy profile indicates that there is a nontrivial but surmountable barrier to the flipping of capsaicin between opposing leaflets of the bilayer. Molecular dynamics of the S1-S4 transmembrane helices of the TRPV1 in a lipid bilayer confirm that Y511, known to be crucial to capsaicin binding, has a distribution along the bilayer normal similar to that of the aromatic group of capsaicin. Simulations were conducted of the TRPV1 S1-S4 transmembrane helices in the presence of capsaicin placed in the aqueous phase, in the lipid, or docked to the protein. No stable interaction between ligand and protein was seen for simulations initiated with capsaicin in the bilayer. However, interactions were seen between TRPV1 and capsaicin starting from the cytosolic aqueous phase, and capsaicin remained stable in the majority of simulations from the docked pose. We discuss the significance of capsaicin flipping from the extracellular to the intracellular leaflet and mechanisms of binding site access by capsaicin.

Dataset Information

Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods.

Publications

Probing the mechanism of interaction between capsaicin and myofibrillar proteins through multispectral, molecular docking, and molecular dynamics simulation methods.

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