Cross-Linking Modifications of Different Phenolic Compounds on Myofibrillar Protein of Common Carp

Tan, Chong; Xu, Qian‐Da; Chen, Nan; He, Qiang; Zeng, Wei

doi:10.1007/s11947-022-02958-2

Cited by 13 publications

(1 citation statement)

References 54 publications

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“…Protein conformation changes have been indicated by endogenous uorescence from Trp and Tyr (Sun et al, 2021;Tan et al, 2023). Figure 4( and ) describes the uorescence spectra of polyphenol-MP complexes at different temperatures.…”

Section: Fluorescence Quenching Mechanismmentioning

confidence: 99%

Integrated multi-spectroscopy and molecular dynamics simulations to explore the interaction mechanism of polyphenols and sea bass myofibrillar protein

Zhu,

Li,

Zhong

et al. 2024

Preprint

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This study aimed to explore the interaction mechanism between five different polyphenols (caffeic acid (CFA), gallic acid (GA), chlorogenic acid (CHA), resveratrol (RES), and catechin (CAT)) with sea bass myofibrillar protein (MP). The multi-spectroscopy results showed that all five polyphenols could spontaneously form new complexes with MP, with a binding molar ratio of 1:1. The interaction between CFA and MP is predominantly electrostatic, while the interaction between GA and MP is mainly hydrophobic. The rest of polyphenols and MP are mediated by hydrogen bonds and van der Waals forces. And molecular dynamics (MD) simulations indicated that CHA-myosin had the strongest structural stability, while CFA-myosin had the tightest binding. In addition, the amino acid Lys-179 was the key residue for the interaction between five polyphenols and myosin. This study contributes to better understanding the interaction between polyphenols and sea bass MP, which could develop the processing of aquatic food products.

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Section: Fluorescence Quenching Mechanismmentioning

confidence: 99%