Defects and Chirality in the Nanoparticle-Directed Assembly of Spherocylindrical Shells of Virus Coat Proteins

• Published in: ACS nano Vol. 12; no. 6; pp. 5323 - 5332
• Main Authors: Zeng, Cheng, Rodriguez Lázaro, Guillermo, Tsvetkova, Irina B, Hagan, Michael F, Dragnea, Bogdan
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 26.06.2018
• Subjects: Bromovirus - chemistry; Capsid Proteins - chemistry; Gold - chemistry; Metal Nanoparticles - chemistry; Microscopy, Atomic Force; Microscopy, Electron, Transmission; Models, Molecular; virus-like particles; chirality; packing; nanoparticle-directed assembly; defects
• ISSN: 1936-0851; 1936-086X; 1936-086X
• DOI: 10.1021/acsnano.8b00069

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.