Multicomponent Protein Cage Architectures for Photocatalysis
Abstract
The central focus of the work performed under this award has been to develop the bacteriophage P22 viral capsid as a vehicle for the encapsulation of catalyticaly active cargo materials and study their utility towards economic energy harvesting systems. We have demonstrated that the capsid of the bacteriophage P22 can be used to genetically program the assembly and encapsulation of a range of inorganic nanoparticles and protein cargoes. The P22 capsid uses a scaffold protein (SP) to direct the assembly of its coat protein (CP) into icosahedral capsids. By creating a genetic fusion of a desired cargo enzyme or a small peptide that can act as a nucleation site for subsequent NP growth, we have demonstrated the co-assembly of these SP-fusions and CP into stable “nano-reactors”. The cargo is sequestered inside the engineered capsid and can either be used directly as a nanocatalyst or for the nucleation and growth of inorganic or organic nanoparticles or polymers. The synthetic cargos (NP or polymers) were shown to have photocatalytic activity. The time dependent photophysics of a select few of these systems were studied to determine the underlying mechanisms and efficiency of light harversting. Enzyme cargos encapsulated within the P22 were thermally activatedmore »
- Authors:
-
- Montana State University
- Publication Date:
- Research Org.:
- Montana State Univ., Bozeman, MT (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1172771
- Report Number(s):
- DOE-MSU-46477
- DOE Contract Number:
- FG02-07ER46477
- Resource Type:
- Technical Report
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 36 MATERIALS SCIENCE; bioinspired materials; biomaterials; virus-like particles
Citation Formats
Douglas, Trevor. Multicomponent Protein Cage Architectures for Photocatalysis. United States: N. p., 2014.
Web. doi:10.2172/1172771.
Douglas, Trevor. Multicomponent Protein Cage Architectures for Photocatalysis. United States. https://doi.org/10.2172/1172771
Douglas, Trevor. 2014.
"Multicomponent Protein Cage Architectures for Photocatalysis". United States. https://doi.org/10.2172/1172771. https://www.osti.gov/servlets/purl/1172771.
@article{osti_1172771,
title = {Multicomponent Protein Cage Architectures for Photocatalysis},
author = {Douglas, Trevor},
abstractNote = {The central focus of the work performed under this award has been to develop the bacteriophage P22 viral capsid as a vehicle for the encapsulation of catalyticaly active cargo materials and study their utility towards economic energy harvesting systems. We have demonstrated that the capsid of the bacteriophage P22 can be used to genetically program the assembly and encapsulation of a range of inorganic nanoparticles and protein cargoes. The P22 capsid uses a scaffold protein (SP) to direct the assembly of its coat protein (CP) into icosahedral capsids. By creating a genetic fusion of a desired cargo enzyme or a small peptide that can act as a nucleation site for subsequent NP growth, we have demonstrated the co-assembly of these SP-fusions and CP into stable “nano-reactors”. The cargo is sequestered inside the engineered capsid and can either be used directly as a nanocatalyst or for the nucleation and growth of inorganic or organic nanoparticles or polymers. The synthetic cargos (NP or polymers) were shown to have photocatalytic activity. The time dependent photophysics of a select few of these systems were studied to determine the underlying mechanisms and efficiency of light harversting. Enzyme cargos encapsulated within the P22 were thermally activated catalysts and their kinetic behavior was characterized. During the course of this work we have demonstrated that the method is a robust means to harness biology for materials applications and have initiated work into assembling the P22 nanoreactors into hierarchically ordered materials. The successful implementation of the work performed under this DOE grant provides us with a great deal of knowledge and a library of components to go forward towards the development of bioinspired catalytic materials for energy harvesting.},
doi = {10.2172/1172771},
url = {https://www.osti.gov/biblio/1172771},
journal = {},
number = ,
volume = ,
place = {United States},
year = {Fri Nov 21 00:00:00 EST 2014},
month = {Fri Nov 21 00:00:00 EST 2014}
}