Adjustment of Protein Crystal Porosity for Biotemplating: Chemical and Protein Engineering Tools

Wine, Yariv; Cohen-Hadar, Noa; Lagziel-Simis, S.; Dror, Yael; Frolow, Felix; Freeman, Amihay

doi:10.1063/1.3453810

Cited by 4 publications

(5 citation statements)

References 24 publications

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“…In 2009 and 2011, Felix Frolow and Amihay Freeman's group used both systematic mutation (Wine, Cohen-Hadar, Lamed, Freeman, & Frolow, 2009) and chemical modification (Cohen-Hadar, Lagziel-Simis, Wine, Frolow, & Freeman, 2011) of pore surface residues to alter the porosity of HEWL crystals in the interest of biotemplating applications. Furthermore, they determined that simple addition of various metal ions (Co 2+ , Ni 2+ , Cu 2+ , Zn 2+ , Cd 2+ ) to the crystal growth environment could provide a strategy to "fine tune" the porosity of the resulting crystal (Wine et al, 2010).…”

Section: Engineering Crystal Surfaces and Pore Environmentsmentioning

confidence: 99%

Protein crystal based materials for nanoscale applications in medicine and biotechnology

Hartje

Snow

2018

WIREs Nanomed Nanobiotechnol

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The porosity, order, biocompatibility, and chirality of protein crystals has motivated interest from diverse research domains including materials science, biotechnology, and medicine. Porous protein crystals have the unusual potential to organize guest molecules within highly ordered scaffolds, enabling applications ranging from biotemplating and catalysis to biosensing and drug delivery. Significant research has therefore been directed toward characterizing protein crystal materials in hopes of optimizing crystallization, scaffold stability, and application efficacy. In this overview article, we describe recent progress in the field of protein crystal materials with special attention given to applications in nanomedicine and nanobiotechnology.

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Section: Engineering Crystal Surfaces and Pore Environmentsmentioning

confidence: 99%

Protein crystal based materials for nanoscale applications in medicine and biotechnology

Hartje

Snow

2018

WIREs Nanomed Nanobiotechnol

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“…To illustrate the feasibility of the latter approach, Wine and coworkers [82,83] used protein engineering tools to modify the packing of a selected protein (cohesin from Acetivibrio cellulolyticus ) as illustrated in Figure 5.…”

Section: Protein Crystal-mediated Biotemplatingmentioning

confidence: 99%

“…( e ) Optical micrograph of a K117W-K119W double mutant protein crystal and ( f ) ribbon representation of its crystal packing (cross-section in bc plane). Reprinted with permission from [83], Copyright 2010, AIP Publishing LLC.…”

Section: Figurementioning

confidence: 99%

Protein-Mediated Biotemplating on the Nanoscale

Freeman

2017

Biomimetics

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Purified proteins offer a homogeneous population of biological nanoparticles, equipped in many cases with specific binding sites enabling the directed self-assembly of envisaged one-, twoor three-dimensional arrays. These arrays may serve as nanoscale biotemplates for the preparation of novel functional composite materials, which exhibit potential applications, especially in the fields of nanoelectronics and optical devices. This review provides an overview of the field of protein-mediated biotemplating, focussing on achievements made throughout the past decade. It is comprised of seven sections designed according to the size and configuration of the protein-made biotemplate. Each section describes the design and size of the biotemplate, the resulting hybrid structures, the fabrication methodology, the analytical tools employed for the structural analysis of the hybrids obtained, and, finally, their claimed/intended applications and a feasibility demonstration (whenever available). In conclusion, a short assessment of the overall status of the achievements already made vs. the future challenges of this field is provided.

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“…One caveat of this fusion-protein strategy is that the linker may prevent the native association mode; for this reason, the linker has to be optimized and the fusion protein has to be characterized, with the observed association mode compared with the native complex in solution, for example by using biophysical techniques and site-directed mutagenesis. An alternative approach to fusing the interacting partners is to cross-link them; however, this alternative approach comes with its own challenges, in particular the heterogeneity introduced by the cross-linking reaction (Reddy Chichili et al, 2013a;Mouradov et al, 2008;Wine et al, 2007;Leitner et al, 2010).…”

Section: Fusion Of Interacting Proteins Approachmentioning

confidence: 99%

Fusion-protein-assisted protein crystallization

Kobe

Williams

2015

Acta Cryst Sect F

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Fusion proteins can be used directly in protein crystallization to assist crystallization in at least two different ways. In one approach, the 'heterologous fusion-protein approach', the fusion partner can provide additional surface area to promote crystal contact formation. In another approach, the 'fusion of interacting proteins approach', protein assemblies can be stabilized by covalently linking the interacting partners. The linker connecting the proteins plays different roles in the two applications: in the first approach a rigid linker is required to reduce conformational heterogeneity; in the second, conversely, a flexible linker is required that allows the native interaction between the fused proteins. The two approaches can also be combined. The recent applications of fusion-protein technology in protein crystallization from the work of our own and other laboratories are briefly reviewed.

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Adjustment of Protein Crystal Porosity for Biotemplating: Chemical and Protein Engineering Tools

Cited by 4 publications

References 24 publications

Protein crystal based materials for nanoscale applications in medicine and biotechnology

Protein crystal based materials for nanoscale applications in medicine and biotechnology

Protein-Mediated Biotemplating on the Nanoscale

Fusion-protein-assisted protein crystallization

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