{"title":"Protein-Based Controllable Nanoarchitectonics for Desired Applications","authors":"Ling Li, Yingying Zhang, Yage Wu, Zhengge Wang, Wandi Cui, Chunhong Zhang, Jinglin Wang, Yongchun Liu, Peng Yang","doi":"10.1002/adfm.202315509","DOIUrl":null,"url":null,"abstract":"<p>Controllable protein nanoarchitectonics refers to the process of manipulating and controlling the assembly of proteins at the nanoscale to achieve domain-limited and accurate spatial arrangement. In nature, many proteins undergo precise self-assembly with other structural domains to engage in synergistic physiological activities. Protein nanomaterials prepared through protein nanosizing have received considerable attention due to their excellent biocompatibility, low toxicity, modifiability, and versatility. This review focuses on the fundamental strategies used for controllable protein nanoarchitectinics, which include computational design, self-assembly induction, template introduction, complexation induction, chemical modification, and in vivo assembly. Precise controlling of the nanosizing process has enabled the creation of protein nanostructures with different dimensions, including 0D spherical oligomers, 1D nanowires, nanorings, and nanotubes, as well as 2D nanofilms, and 3D protein nanocages. The unique biological properties of proteins hold promise for diverse applications of these protein nanomaterials, including in biomedicine, the food industry, agriculture, biosensing, environmental protection, biocatalysis, and artificial light harvesting. Protein nanosizing is a powerful tool for developing biomaterials with advanced structures and functions.</p>","PeriodicalId":112,"journal":{"name":"Advanced Functional Materials","volume":null,"pages":null},"PeriodicalIF":18.5000,"publicationDate":"2024-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Advanced Functional Materials","FirstCategoryId":"88","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/adfm.202315509","RegionNum":1,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0
Abstract
Controllable protein nanoarchitectonics refers to the process of manipulating and controlling the assembly of proteins at the nanoscale to achieve domain-limited and accurate spatial arrangement. In nature, many proteins undergo precise self-assembly with other structural domains to engage in synergistic physiological activities. Protein nanomaterials prepared through protein nanosizing have received considerable attention due to their excellent biocompatibility, low toxicity, modifiability, and versatility. This review focuses on the fundamental strategies used for controllable protein nanoarchitectinics, which include computational design, self-assembly induction, template introduction, complexation induction, chemical modification, and in vivo assembly. Precise controlling of the nanosizing process has enabled the creation of protein nanostructures with different dimensions, including 0D spherical oligomers, 1D nanowires, nanorings, and nanotubes, as well as 2D nanofilms, and 3D protein nanocages. The unique biological properties of proteins hold promise for diverse applications of these protein nanomaterials, including in biomedicine, the food industry, agriculture, biosensing, environmental protection, biocatalysis, and artificial light harvesting. Protein nanosizing is a powerful tool for developing biomaterials with advanced structures and functions.
期刊介绍:
Firmly established as a top-tier materials science journal, Advanced Functional Materials reports breakthrough research in all aspects of materials science, including nanotechnology, chemistry, physics, and biology every week.
Advanced Functional Materials is known for its rapid and fair peer review, quality content, and high impact, making it the first choice of the international materials science community.