Altering the energy landscape of virus self-assembly to generate kinetically trapped nanoparticles.
Controlling self-assembly is critical to the advancement of nanotechnology. A rugged or crenated assembly energy surface can redirect assembly off path. By using a defined starting point and an energy surface made rough by a strong association energy, we can impose entirely new assembly paths and products. Normally, the coat protein (CP) of the Cowpea Chlorotic Mottle Virus (CCMV) assembles into virus-like 28 nm diameter icosahedral particles. Here we have started with the coat protein trapped in a rod-like structure in complex with DNA. When these 17 nm diameter rods are placed under the same condition, low pH, that normally leads to assembly of 28 nm diameter particles, we instead obtain 17 nm capsids. The extrusion of all-pentamer capsids from the hexagonal lattice of the rod demonstrates the importance of the starting state for controlled assembly.
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, 73104, USA.
Kevin
K
Burns
Santanu
S
Mukherjee
Thomas
T
Keef
Jennifer M
JM
Johnson
Adam
A
Zlotnick
D017795:Bromovirus / Q000737:chemistry* / Q000502:physiology*; D036022:Capsid Proteins / Q000737:chemistry / Q000502:physiology; D004735:Energy Transfer / Q000502:physiology; D053758:Nanoparticles / Q000737:chemistry*; D013499:Surface Properties; D019065:Virus Assembly / Q000502:physiology*
D036022:Capsid Proteins