Abstract
Diverse natural/artificial proteins have been used as building blocks to construct a variety of well-ordered nanoscale structures over the past couple of decades. Sophisticated protein self-assemblies have attracted great scientific interests due to their potential applications in disease diagnosis, illness treatment, biomechanics, bio-optics and bio-electronics, etc. This review outlines recent efforts directed to the creation of structurally defined protein assemblies including one-dimensional (1D) strings/rings/tubules, two-dimensional (2D) planar sheets and three-dimensional (3D) polyhedral scaffolds. We elucidate various innovative strategies for manipulating proteins to self-assemble into desired architectures. The emergent applications of protein assemblies as versatile platforms in medicine and material science with improved performances have also been discussed.
Highlights
The self-assembly of proteins into an enormous range of molecular machines and structural scaffolds is one of the core principles for nature to create countless organisms, such as the oligomerization of protein kinases, transmembrane proteins, and signaling proteins, the polymerization of cytoskeletal proteins into intermediate filaments, and the emergence of membrane-less organelles induced by the phase separation of proteins (Nussinov et al, 2015; Boeynaems et al, 2018)
One of the most notorious problems is the robustness of the de novo design of protein origami
The DNA strands within a DNA origami are typically organized in antiparallel
Summary
The self-assembly of proteins into an enormous range of molecular machines and structural scaffolds is one of the core principles for nature to create countless organisms, such as the oligomerization of protein kinases, transmembrane proteins, and signaling proteins, the polymerization of cytoskeletal proteins into intermediate filaments, and the emergence of membrane-less organelles induced by the phase separation of proteins (Nussinov et al, 2015; Boeynaems et al, 2018). The spindle assembly abnormal protein 6 (SAS-6), an essential component in the centrioles, is folded to be a central seven-stranded antiparallel open twisted β-sheet flanked by three α-helices (Hilbert et al, 2013). Two helices and five β-strands of them are packed into an N-terminal globular domain, whereas a long α-helix and two β-strands constitute the C-terminal domain
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