Lysozyme amyloid fibril: Regulation, application, hazard analysis, and future perspectives

Yulun Chen; Qingrun Liu; Fangwei Yang; Hang Yu; Yunfei Xie; Weirong Yao

doi:10.1016/j.ijbiomac.2021.12.163

Lysozyme amyloid fibril: Regulation, application, hazard analysis, and future perspectives

Int J Biol Macromol. 2022 Mar 1:200:151-161. doi: 10.1016/j.ijbiomac.2021.12.163. Epub 2022 Jan 4.

Authors

Yulun Chen¹, Qingrun Liu², Fangwei Yang¹, Hang Yu², Yunfei Xie¹, Weirong Yao³

Affiliations

¹ State Key Laboratory of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; Engineering Research Center of Dairy Quality and Safety Control Technology, Ministry of Education, Inner Mongolia University, No.235 Daxue West Road, Hohhot 010021, Inner Mongolia Autonomous Region, China; School of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; Joint International Research Laboratory of Food Safety, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China.
² State Key Laboratory of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; School of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; Joint International Research Laboratory of Food Safety, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China.
³ State Key Laboratory of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; School of Food Science and Technology, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China; Joint International Research Laboratory of Food Safety, Jiangnan University, No.1800 Lihu Avenue, Wuxi 214122, Jiangsu Province, China. Electronic address: yaoweirongcn@jiangnan.edu.cn.

PMID: 34995654
DOI: 10.1016/j.ijbiomac.2021.12.163

Abstract

Self-assembly of misfolded proteins into ordered fibrillar aggregates known as amyloid results in various human diseases. However, more and more proteins, whether in human body or in food, have been found to be able to form amyloid fibrils with in-depth researches. As a model protein for amyloid research, lysozyme has always been the focus of research in various fields. Firstly, the formation mechanisms of amyloid fibrils are discussed concisely. Researches on the regulation of lysozyme amyloid fibrils are helpful to find suitable therapeutic drugs and unfriendly substances. And this review article summarizes a number of exogenous substances including small molecules, nanoparticles, macromolecules, and polymers. Small molecules are mainly connected to lysozyme through hydrophobic interaction, electrostatic interaction, π-π interaction, van der Waals force and hydrogen bond. Nanoparticles inhibit the formation of amyloid fibers by stabilizing lysozyme and fixing β-sheet. Besides, the applications of lysozyme amyloid fibrils in food-related fields are considered furtherly due to outstanding physical and mechanical properties. Nevertheless, the potential health threats are still worthy of our attention. Finally, we also give suggestions and opinions on the future research direction of lysozyme amyloid fibrils.

Keywords: Amyloid fibril; Health implications; Protein aggregation; Regulation; Techno-functional properties.

Publication types

Review

MeSH terms

Amyloid*

Substances

Amyloid