Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods
Ferulic acid (FA) and ferulic acid methyl ester (FAM) are important phenolic compounds in Baijiu. In this study, the interaction of FA and FAM with human serum albumin (HSA) and lysozyme (LZM) was investigated using multispectral methods and molecular dynamics simulation. FA and FAM could interact w...
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Elsevier
2024-01-01
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author | Ying Yang Shuqin Wang Xingyan Liu Wenbin Zhang Wenhua Tong Huibo Luo Liming Zhao |
author_facet | Ying Yang Shuqin Wang Xingyan Liu Wenbin Zhang Wenhua Tong Huibo Luo Liming Zhao |
author_sort | Ying Yang |
collection | DOAJ |
description | Ferulic acid (FA) and ferulic acid methyl ester (FAM) are important phenolic compounds in Baijiu. In this study, the interaction of FA and FAM with human serum albumin (HSA) and lysozyme (LZM) was investigated using multispectral methods and molecular dynamics simulation. FA and FAM could interact with HSA and LZM, changing the conformation and hydrophilicity of the protein. The quenching mechanisms of FA-HSA, FA-LZM, FAM-HSA, and FAM-LZM were all static-quenching. In the FA-HSA, FAM-HSA, and FA-LZM systems, the interaction forces were mainly hydrophobic interactions and hydrogen bonding. In the FAM-LZM system, the interaction forces were mainly hydrophobic interactions, hydrogen bonding, and van der Waals force. Common metal ions such as K+, Ca2+, Cu2+, Mg2+, and Mn2+ could affect the binding ability of FA and FAM to HSA and LZM. Moreover, FA and FAM could increase the stability of HSA and LZM, and the protein bound to FA/FAM was more stable than the free protein. FA and FAM had varying degrees of impact on the physiological activities of HSA and LZM. This study provides relevant information on the interactions and metabolic mechanisms of FA and its derivatives with endogenous proteins. |
first_indexed | 2024-03-08T06:55:06Z |
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institution | Directory Open Access Journal |
issn | 2405-8440 |
language | English |
last_indexed | 2024-03-08T06:55:06Z |
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spelling | doaj.art-8bc79a4553434af8b47afa77b5d5d3562024-02-03T06:37:58ZengElsevierHeliyon2405-84402024-01-01102e24605Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methodsYing Yang0Shuqin Wang1Xingyan Liu2Wenbin Zhang3Wenhua Tong4Huibo Luo5Liming Zhao6School of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, ChinaSchool of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, ChinaSchool of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, ChinaGuangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, College of Life Sciences, South China Agricultural University, Guangzhou, 510000, ChinaSchool of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, China; Key Laboratory of Brewing Biotechnology and Application, Yibin, 644000, China; Corresponding author. School of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, China.tongwh@suse.edu.cnSchool of Biological Engineering, Sichuan University of Science and Engineering, Yibin, 644000, China; Key Laboratory of Brewing Biotechnology and Application, Yibin, 644000, ChinaEast China University of Science and Technology, Shanghai, 200000, China; Corresponding author.Ferulic acid (FA) and ferulic acid methyl ester (FAM) are important phenolic compounds in Baijiu. In this study, the interaction of FA and FAM with human serum albumin (HSA) and lysozyme (LZM) was investigated using multispectral methods and molecular dynamics simulation. FA and FAM could interact with HSA and LZM, changing the conformation and hydrophilicity of the protein. The quenching mechanisms of FA-HSA, FA-LZM, FAM-HSA, and FAM-LZM were all static-quenching. In the FA-HSA, FAM-HSA, and FA-LZM systems, the interaction forces were mainly hydrophobic interactions and hydrogen bonding. In the FAM-LZM system, the interaction forces were mainly hydrophobic interactions, hydrogen bonding, and van der Waals force. Common metal ions such as K+, Ca2+, Cu2+, Mg2+, and Mn2+ could affect the binding ability of FA and FAM to HSA and LZM. Moreover, FA and FAM could increase the stability of HSA and LZM, and the protein bound to FA/FAM was more stable than the free protein. FA and FAM had varying degrees of impact on the physiological activities of HSA and LZM. This study provides relevant information on the interactions and metabolic mechanisms of FA and its derivatives with endogenous proteins.http://www.sciencedirect.com/science/article/pii/S2405844024006364Ferulic acidFerulic acid methyl esterHuman serum albuminLysozymeMolecular dynamics simulationsResonance light scattering |
spellingShingle | Ying Yang Shuqin Wang Xingyan Liu Wenbin Zhang Wenhua Tong Huibo Luo Liming Zhao Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods Heliyon Ferulic acid Ferulic acid methyl ester Human serum albumin Lysozyme Molecular dynamics simulations Resonance light scattering |
title | Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods |
title_full | Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods |
title_fullStr | Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods |
title_full_unstemmed | Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods |
title_short | Interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins: Determination using the multi-methods |
title_sort | interactions of ferulic acid and ferulic acid methyl ester with endogenous proteins determination using the multi methods |
topic | Ferulic acid Ferulic acid methyl ester Human serum albumin Lysozyme Molecular dynamics simulations Resonance light scattering |
url | http://www.sciencedirect.com/science/article/pii/S2405844024006364 |
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