Journal
FOOD SCIENCE AND HUMAN WELLNESS
Volume 11, Issue 2, Pages 199-207Publisher
KEAI PUBLISHING LTD
DOI: 10.1016/j.fshw.2021.11.001
Keywords
PROTAC; Ligand; Natural products; Target binding
Categories
Funding
- key scientific research projects of Hunan Provincial Department of Education of China [19A513]
- National Nonprofit Institute Research Grant of CAFINT, China [CAFYBB2018GA001]
- Hubei Province, China [2019ABA100]
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PROTAC technology allows for direct degradation of target proteins and has broad applications.
There are numerous evaluations of natural products, of which majority are food bioactives, performed up to date for their various health beneficial activities via targeting specific proteins. However, the direct identification of a targeted protein remains unexplored for natural occurring compounds. Proteolysis targeting chimera (PROTAC) is a type of bifunctional chimeric molecules that can directly degrade the binding proteins targeted by bioactive molecules in an ubiquitin-proteasome pathway. As the agents in protein degradation dependent on ubiquitin ligase, the bifunctional molecule connects the target protein ligand and E3 ligase ligand together via an appropriate linker. It is highly selective and efficient to induce the ubiquitin-mediated degradation of targeted binding proteins. Therefore, it has been demonstrated that the PROTAC technology has broad application in the modulation of the target protein level. In this review, we outlined the advances in PROTAC combined molecule compounds, summarized its quantitative structure-activity relationship, and finally reviewed the methods applied in identifying the target proteins of natural products. We hope it will provide an insightful application of PROTAC techniques in the target protein identification of natural products including food bioactive molecules. (c) 2022 Beijing Academy of Food Sciences. Publishing services by Elsevier B.V. on behalf of KeAi Communications Co., Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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