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利用残基特异性非天然氨基酸掺入工程化蛋白质和材料。

Engineered Proteins and Materials Utilizing Residue-Specific Noncanonical Amino Acid Incorporation.

机构信息

Department of Chemical and Biomolecular Engineering, New York University Tandon School of Engineering, Brooklyn, New York 11201, United States.

Department of Biomedical Engineering, New York University Tandon School of Engineering, Brooklyn, New York 11201, United States.

出版信息

Chem Rev. 2024 Aug 14;124(15):9113-9135. doi: 10.1021/acs.chemrev.3c00855. Epub 2024 Jul 15.

DOI:10.1021/acs.chemrev.3c00855
PMID:39008623
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11327963/
Abstract

The incorporation of noncanonical amino acids into proteins and protein-based materials has significantly expanded the repertoire of available protein structures and chemistries. Through residue-specific incorporation, protein properties can be globally modified, resulting in the creation of novel proteins and materials with diverse and tailored characteristics. In this review, we highlight recent advancements in residue-specific incorporation techniques as well as the applications of the engineered proteins and materials. Specifically, we discuss their utility in bio-orthogonal noncanonical amino acid tagging (BONCAT), fluorescent noncanonical amino acid tagging (FUNCAT), threonine-derived noncanonical amino acid tagging (THRONCAT), cross-linking, fluorination, and enzyme engineering. This review underscores the importance of noncanonical amino acid incorporation as a tool for the development of tailored protein properties to meet diverse research and industrial needs.

摘要

将非天然氨基酸掺入蛋白质和基于蛋白质的材料中，极大地扩展了可用蛋白质结构和化学物质的范围。通过残基特异性掺入，可以全局修饰蛋白质性质，从而创建具有各种定制特性的新型蛋白质和材料。在这篇综述中，我们重点介绍了残基特异性掺入技术的最新进展，以及工程化蛋白质和材料的应用。具体而言，我们讨论了它们在生物正交非天然氨基酸标记（BONCAT）、荧光非天然氨基酸标记（FUNCAT）、苏氨酸衍生非天然氨基酸标记（THRONCAT）、交联、氟化和酶工程中的应用。本综述强调了非天然氨基酸掺入作为一种开发定制蛋白质性质的工具的重要性，以满足不同的研究和工业需求。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/d58f60b2d859/cr3c00855_0014.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/d41d75717bc8/cr3c00855_0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/a2c9b3f562bf/cr3c00855_0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/cd9379564d23/cr3c00855_0011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/7ca7a961026e/cr3c00855_0012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/a64b4d52b391/cr3c00855_0013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/d58f60b2d859/cr3c00855_0014.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/4921f2ea482b/cr3c00855_0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/05a5140c74ab/cr3c00855_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/6899ed7bf6ac/cr3c00855_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/5bae99fe16d4/cr3c00855_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/403743492351/cr3c00855_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/2d973ef58476/cr3c00855_0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/5ff870ad681c/cr3c00855_0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/304ec7c10860/cr3c00855_0008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/d41d75717bc8/cr3c00855_0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/a2c9b3f562bf/cr3c00855_0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/cd9379564d23/cr3c00855_0011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/7ca7a961026e/cr3c00855_0012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/a64b4d52b391/cr3c00855_0013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2ec0/11327963/d58f60b2d859/cr3c00855_0014.jpg

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