Journal: Biomacromolecules / Year: 2018 Title: Cargo Retention inside P22 Virus-Like Particles. Authors: Kimberly McCoy / Ekaterina Selivanovitch / Daniel Luque / Byeongdu Lee / Ethan Edwards / José R Castón / Trevor Douglas / Abstract: Viral protein cages, with their regular and programmable architectures, are excellent platforms for the development of functional nanomaterials. The ability to transform a virus into a material with ...Viral protein cages, with their regular and programmable architectures, are excellent platforms for the development of functional nanomaterials. The ability to transform a virus into a material with intended structure and function relies on the existence of a well-understood model system, a noninfectious virus-like particle (VLP) counterpart. Here, we study the factors important to the ability of P22 VLP to retain or release various protein cargo molecules depending on the nature of the cargo, the capsid morphology, and the environmental conditions. Because the interaction between the internalized scaffold protein (SP) and the capsid coat protein (CP) is noncovalent, we have studied the efficiency with which a range of SP variants can dissociate from the interior of different P22 VLP morphologies and exit by traversing the porous capsid. Understanding the types of cargos that are either retained or released from the P22 VLP will aid in the rational design of functional nanomaterials.
History
Deposition
Apr 19, 2018
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Header (metadata) release
May 23, 2018
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Map release
Aug 22, 2018
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Update
Sep 19, 2018
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Current status
Sep 19, 2018
Processing site: PDBe / Status: Released
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