Fibrous Nanostructures from the Self‐Assembly of Designed Repeat Protein Modules

Phillips, Jonathan J.; Millership, Charlotte; Main, Ewan R. G.

doi:10.1002/ange.201203795

Cited by 11 publications

(11 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[29][30][31][32] We have recently used these modules to show the specific functionalization of patterned polymeric surfaces. [33,34] Moreover, it has been shown that under certain conditions CTPR proteins self-assemble into ordered structures including ordered protein films comprised, [35] and linear nanofibers in solution [36,37], mimicking the packing observed in the crystal forms of CTPRs. [27,28,38] These results illustrate the potential of these protein modules as self-assembling building blocks.…”

Section: Introductionmentioning

confidence: 99%

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Mejías

Couleaud

Casado

et al. 2016

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

The controlled assembly of building blocks to achieve new nanostructured materials with defined properties at different length scales through rational design is the basis and future of bottom-up nanofabrication. This work describes the assembly of the idealized protein building block, the consensus tetratricopeptide repeat (CTPR), into monolayers by oriented immobilization of the blocks. The selectivity of thiol-gold interaction for an oriented immobilization has been verified by comparing a non-thiolated protein building block. The physical properties of the CTPR protein thin biomolecular films including topography, thickness, and viscoelasticity, are characterized. Finally, the ability of these scaffolds to act as templates for inorganic nanostructures has been demonstrated by the formation of well-packed gold nanoparticles (GNPs) monolayer patterned by the CTPR monolayer.

show abstract

Section: Introductionmentioning

confidence: 99%

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Mejías

Couleaud

Casado

et al. 2016

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

show abstract

“…A protein with a pair of binding partners on opposite sides would polymerize controllably in a manner depending on the nature of the binding partners. This strategy has been used previously [16][17][18][19][20][21][22][23] , but there remained several problems: for example, chemical modifications of monomers to make binding sites are often necessary [16][17][18][19][20] , single strands of the polymers are supposed to break easily and to be not stable for long periods in dilute solution because they are held together by noncovalent interactions 16,17,[21][22][23] , and single strands of the polymers often assemble in an uncontrolled manner 21,22 .…”

mentioning

confidence: 99%

Hyperthin nanochains composed of self-polymerizing protein shackles

et al. 2013

View full text Add to dashboard Cite

Protein fibrils are expected to have applications as functional nanomaterials because of their sophisticated structures; however, nanoscale ordering of the functional units of protein fibrils remains challenging. Here we design a series of self-polymerizing protein monomers, referred to as protein shackles, derived from modified recombinant subunits of pili from Streptococcus pyogenes. The monomers polymerize into nanochains through spontaneous irreversible covalent bond formation. We design the protein shackles so that their reactions can be controlled by altering redox conditions, which affect disulphide bond formation between engineered cysteine residues. The interaction between the monomers improves their polymerization reactivity and determines morphologies of the polymers. In addition, green fluorescent protein-tagged protein shackles can polymerize, indicating proteins can be stably attached to the nanochains with its functionality preserved. Furthermore we demonstrate that a molecular-recognizable nanochain binds to its partner with an enhanced binding ability in solution. These characteristics are expected to be applied for novel protein nanomaterials.

show abstract

“…In particular, we have incorporated the ability to fit and simulate equilibrium unfolding experiments with user defined protein topologies, using a matrix formulation of the 1-D heteropolymer Ising model. This aspect of PyFolding will be of particular interest to groups working on protein folds composed of repetitive motifs such as Ankyrin repeats and tetratricopeptide repeats, given that these proteins are increasingly being used as novel antibody therapeutics (38)(39)(40)(41) and biomaterials (42)(43)(44)(45)(46)(47). Further, as analysis can be performed in Jupyter notebooks, it enables novice researchers to easily use the software and for groups to share data and methods.…”

Section: Discussionmentioning

confidence: 99%

PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins

Lowe

Perez-Riba

Itzhaki

et al. 2018

Biophysical Journal

View full text Add to dashboard Cite

For many years, curve-fitting software has been heavily utilized to fit simple models to various types of biophysical data. Although such software packages are easy to use for simple functions, they are often expensive and present substantial impediments to applying more complex models or for the analysis of large data sets. One field that is reliant on such data analysis is the thermodynamics and kinetics of protein folding. Over the past decade, increasingly sophisticated analytical models have been generated, but without simple tools to enable routine analysis. Consequently, users have needed to generate their own tools or otherwise find willing collaborators. Here we present PyFolding, a free, open-source, and extensible Python framework for graphing, analysis, and simulation of the biophysical properties of proteins. To demonstrate the utility of PyFolding, we have used it to analyze and model experimental protein folding and thermodynamic data. Examples include: 1) multiphase kinetic folding fitted to linked equations, 2) global fitting of multiple data sets, and 3) analysis of repeat protein thermodynamics with Ising model variants. Moreover, we demonstrate how PyFolding is easily extensible to novel functionality beyond applications in protein folding via the addition of new models. Example scripts to perform these and other operations are supplied with the software, and we encourage users to contribute notebooks and models to create a community resource. Finally, we show that PyFolding can be used in conjunction with Jupyter notebooks as an easy way to share methods and analysis for publication and among research teams.

show abstract

Fibrous Nanostructures from the Self‐Assembly of Designed Repeat Protein Modules

Cited by 11 publications

References 34 publications

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Assembly of designed protein scaffolds into monolayers for nanoparticle patterning

Hyperthin nanochains composed of self-polymerizing protein shackles

PyFolding: Open-Source Graphing, Simulation, and Analysis of the Biophysical Properties of Proteins

Contact Info

Product

Resources

About