AI Article Synopsis
- The study focuses on how virus coat proteins, typically forming symmetric icosahedral shapes, can also assemble into different structures like spherocylindrical shells around metal nanorods.
- By analyzing the assembly process using atomic force microscopy and molecular dynamics models, the research reveals how chiral angles and packing defects contribute to the growth of these structures.
- The findings suggest potential applications for virus coat proteins in nanotechnology, particularly for creating shells with less symmetry than traditional icosahedrons.
Article Abstract
Virus coat proteins of small isometric plant viruses readily assemble into symmetric, icosahedral cages encapsulating noncognate cargo, provided the cargo meets a minimal set of chemical and physical requirements. While this capability has been intensely explored for certain virus-enabled nanotechnologies, additional applications require lower symmetry than that of an icosahedron. Here, we show that the coat proteins of an icosahedral virus can efficiently assemble around metal nanorods into spherocylindrical closed shells with hexagonally close-packed bodies and icosahedral caps. Comparison of chiral angles and packing defects observed by in situ atomic force microscopy with those obtained from molecular dynamics models offers insight into the mechanism of growth, and the influence of stresses associated with intrinsic curvature and assembly pathways.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6202266 | PMC |
| http://dx.doi.org/10.1021/acsnano.8b00069 | DOI Listing |
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