Highly ordered protein cage assemblies: A toolkit for new materials

被引:45
作者
Korpi, Antti [1 ]
Anaya-Plaza, Eduardo [1 ]
Valimaki, Salla [1 ]
Kostiainen, Mauri [1 ]
机构
[1] Aalto Univ, Dept Bioprod & Biosyst, Biohybrid Mat, Aalto 00076, Finland
基金
欧盟地平线“2020”;
关键词
biohybrid; protein assembly; proteincage; self-assembly; supramolecular interactions; TOBACCO-MOSAIC-VIRUS; CRYSTAL-STRUCTURE; PHAGE DISPLAY; ENGINEERED PROTEIN; GOLD NANOPARTICLES; METAL COORDINATION; CHAPERONIN GROEL; OXIDATIVE STRESS; STRUCTURAL BASIS; ENERGY-TRANSFER;
D O I
10.1002/wnan.1578
中图分类号
TB3 [工程材料学];
学科分类号
0805 ; 080502 ;
摘要
Protein capsids are specialized and versatile natural macromolecules with exceptional properties. Their homogenous, spherical, rod-like or toroidal geometry, and spatially directed functionalities make them intriguing building blocks for self-assembled nanostructures. High degrees of functionality and modifiability allow for their assembly via non-covalent interactions, such as electrostatic and coordination bonding, enabling controlled self-assembly into higher-order structures. These assembly processes are sensitive to the molecules used and the surrounding conditions, making it possible to tune the chemical and physical properties of the resultant material and generate multifunctional and environmentally sensitive systems. These materials have numerous potential applications, including catalysis and drug delivery. This article is categorized under: Biology-Inspired Nanomaterials > Protein and Virus-Based Structures
引用
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页数:24
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