Fabrication of Nanoreaction Clusters with Dual-Functionalized Protein Cage Nanobuilding Blocks

Small ◽  
2018 ◽  
Vol 14 (35) ◽  
pp. 1801488 ◽  
Author(s):  
Hyukjun Choi ◽  
Bongseo Choi ◽  
Gwang Joong Kim ◽  
Han-ul Kim ◽  
Hansol Kim ◽  
...  
2013 ◽  
Vol 1 (35) ◽  
pp. 4504 ◽  
Author(s):  
Hyojin Moon ◽  
Woo Gyum Kim ◽  
Seongdong Lim ◽  
Young Ji Kang ◽  
Hyun-Hee Shin ◽  
...  

2018 ◽  
Author(s):  
Daniel D. Brauer ◽  
Emily C. Hartman ◽  
Daniel L.V. Bader ◽  
Zoe N. Merz ◽  
Danielle Tullman-Ercek ◽  
...  

<div> <p>Site-specific protein modification is a widely-used strategy to attach drugs, imaging agents, or other useful small molecules to protein carriers. N-terminal modification is particularly useful as a high-yielding, site-selective modification strategy that can be compatible with a wide array of proteins. However, this modification strategy is incompatible with proteins with buried or sterically-hindered N termini, such as virus-like particles like the well-studied MS2 bacteriophage coat protein. To assess VLPs with improved compatibility with these techniques, we generated a targeted library based on the MS2-derived protein cage with N-terminal proline residues followed by three variable positions. We subjected the library to assembly, heat, and chemical selections, and we identified variants that were modified in high yield with no reduction in thermostability. Positive charge adjacent to the native N terminus is surprisingly beneficial for successful extension, and over 50% of the highest performing variants contained positive charge at this position. Taken together, these studies described nonintuitive design rules governing N-terminal extensions and identified successful extensions with high modification potential.</p> </div>


2009 ◽  
Vol 37 (4) ◽  
pp. 665-670 ◽  
Author(s):  
David J. Evans

CPMV (cowpea mosaic virus), a plant virus, is a naturally occurring sphere-like nanoparticle, and is used as a synthon and/or template in bionanoscience. The virions formed by CPMV can be regarded as programmable nanobuilding blocks with a diameter of ∼30 nm. A range of molecules have been attached to this viral nanoscaffold, yielding stable nanoparticles that display multiple copies of the desired molecule. It has been shown that, in addition to surface amine groups, surface carboxy groups are also addressable, and a procedure has been developed that enables introduction of reactive thiols at the virion surface that avoids virus aggregation. Furthermore, the virions can be functionalized to form electroactive nanoparticles. Methods for the construction of arrays and multilayers, using a layer-by-layer approach, have been established. As proof of concept, for example, CPMV particles have been immobilized on surfaces and arranged in defined layers. Engineered variants of CPMV can be used as templates for mineralization with, for example, silica to give monodisperse robust silica nanoparticles of ∼32 nm. SIRV2 (Sulfolobus islandicus rod-shaped virus 2), is a robust archaeal virus, resistant to high temperature and low pH. SIRV2 can act as a template for site-selective and spatially controlled chemical modification. Both the ends and the body of the virus, or the ends only, can be chemically addressed; SIRV2 can be regarded as a structurally unique nanobuilding block.


2010 ◽  
Vol 122 (39) ◽  
pp. 7168-7172 ◽  
Author(s):  
Thomas W. Ni ◽  
F. Akif Tezcan

2003 ◽  
Vol 42 (20) ◽  
pp. 6300-6305 ◽  
Author(s):  
Mark Allen ◽  
Debbie Willits ◽  
Mark Young ◽  
Trevor Douglas

2020 ◽  
Author(s):  
Nikola Lončar ◽  
Henriette J. Rozeboom ◽  
Linda E. Franken ◽  
Marc C. A. Stuart ◽  
Marco Fraaije

In this paper, we report on the discovery of a novel, robust protein cage (encapsulin) that we could use for packaging various biocatalysts. We have elucidated the structure of the stable encapsulin by electron microscopy and X-ray diffraction. Furthermore, we developed an effective expression system for the encapsulin and a facile protocol for preparing encapsulated enzymes. By packaging and testing various enzymes (varying in size, oligomeric structure, and cofactor type) we demonstrate that, through encapsulation, the enzymes become significantly more stable. We also provide evidence that the pores of the encapsulin, through a size-exclusion effect, can modulate the substrate acceptance profile of an encapsulated enzyme.


Biochemistry ◽  
2018 ◽  
Vol 57 (5) ◽  
pp. 604-613 ◽  
Author(s):  
Thomas A. Cornell ◽  
Maziar S. Ardejani ◽  
Jing Fu ◽  
Stephanie H. Newland ◽  
Yu Zhang ◽  
...  

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