Title: Protein Assembly by Design

Journal Article · · Chemical Reviews

Proteins are nature’s primary building blocks for the construction of sophisticated molecular machines and dynamic materials, ranging from protein complexes such as photosystem II and nitrogenase that drive biogeochemical cycles to cytoskeletal assemblies and muscle fibers for motion. Such natural systems have inspired extensive efforts in the rational design of artificial protein assemblies in the last two decades. As molecular building blocks, proteins are highly complex, in terms of both their three-dimensional structures and chemical compositions. To enable control over the self-assembly of such complex molecules, scientists have devised many creative strategies by combining tools and principles of experimental and computational biophysics, supramolecular chemistry, inorganic chemistry, materials science, and polymer chemistry, among others. Owing to these innovative strategies, what started as a purely structure-building exercise two decades ago has, in short order, led to artificial protein assemblies with unprecedented structures and functions and protein-based materials with unusual properties. Furthermore, our goal in this review is to give an overview of this exciting and highly interdisciplinary area of research, first outlining the design strategies and tools that have been devised for controlling protein self-assembly, then describing the diverse structures of artificial protein assemblies, and finally highlighting the emergent properties and functions of these assemblies.

Research Organization:
Univ. of Washington, Seattle, WA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
SC0019288
OSTI ID:
1841020
Journal Information:
Chemical Reviews, Journal Name: Chemical Reviews Journal Issue: 22 Vol. 121; ISSN 0009-2665
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English

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The amyloid state and its association with protein misfolding diseases
  • Knowles, Tuomas P. J.; Vendruscolo, Michele; Dobson, Christopher M.
  • Nature Reviews Molecular Cell Biology, Vol. 15, Issue 6 https://doi.org/10.1038/nrm3810
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