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

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

doi:10.1002/anie.201203795

Cited by 35 publications

(43 citation statements)

References 35 publications

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“…These self-assembly properties have been recently exploited to generate different CTPR-based assemblies, including hydrogels, nanofibres and thin films ( Figure 2) [38][39][40][41]. Protein thin nanofibres were obtained taking advantage of the head-to-tail interactions between proteins to drive the polymerization of the CTPR units ( Figure 2).…”

Section: Supramolecular Assemblies Based On Repeat Proteinsmentioning

confidence: 99%

“…Protein thin nanofibres were obtained taking advantage of the head-to-tail interactions between proteins to drive the polymerization of the CTPR units ( Figure 2). Specific reactivities are introduced at both N-and C-terminal ends of the proteins in different ways to act as staple of the interaction [39,40]. The detailed characterization and modelling of the step growth polymerization process will allow to achieve full control in the fibre formation [39] and the generation of nanorods of defined lengths.…”

Section: Supramolecular Assemblies Based On Repeat Proteinsmentioning

confidence: 99%

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Biomolecular templating of functional hybrid nanostructures using repeat protein scaffolds

Romera

Couleaud

Mejías

et al. 2015

Biochemical Society Transactions

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The precise synthesis of materials and devices with tailored complex structures and properties is a requisite for the development of the next generation of products based on nanotechnology. Nowadays, the technology for the generation of this type of devices lacks the precision to determine their properties and is accomplished mostly by 'trial and error' experimental approaches. The use of bottom-up approaches that rely on highly specific biomolecular interactions of small and simple components is an attractive approach for the templating of nanoscale elements. In nature, protein assemblies define complex structures and functions. Engineering novel bio-inspired assemblies by exploiting the same rules and interactions that encode the natural diversity is an emerging field that opens the door to create nanostructures with numerous potential applications in synthetic biology and nanotechnology. Self-assembly of biological molecules into defined functional structures has a tremendous potential in nano-patterning and the design of novel materials and functional devices. Molecular self-assembly is a process by which complex 3D structures with specified functions are constructed from simple molecular building blocks. Here we discuss the basis of biomolecular templating, the great potential of repeat proteins as building blocks for biomolecular templating and nano-patterning. In particular, we focus on the designed consensus tetratricopeptide repeats (CTPRs), the control on the assembly of these proteins into higher order structures and their potential as building blocks in order to generate functional nanostructures and materials.

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Section: Supramolecular Assemblies Based On Repeat Proteinsmentioning

confidence: 99%

Section: Supramolecular Assemblies Based On Repeat Proteinsmentioning

confidence: 99%

Biomolecular templating of functional hybrid nanostructures using repeat protein scaffolds

Romera

Couleaud

Mejías

et al. 2015

Biochemical Society Transactions

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“…are indicated by different shaped pieces. Examples of published triggers for association are (A and H) chemical-induced polymerization of CTPR modules using native chemical ligation and disulfide bond formation [27,28], (B and H) metal-induced polymerization using minimized β-roll motifs on addition of La 2 + [30], (C and I) thick film formation after large, rigid super-helical 18 CTPR module proteins were deposited on a teflon surface with a plasticizer and left to dry (rectangles of alternating blue and green of three module units denote the extending super-helix [31]), (D and J) hydrogel formation of the same CTPR18 combining with multivalent cognate peptide-PEG cross-linker (pink circles on black lines) [26], (E and K) reversible gelation of a chimera of a leucine zipper (black and red rectangles) with designed minimized β-roll motifs. On addition of Ca 2 + (yellow circles) the minimized β-roll motifs fold (green squares) from unstructured polypeptides and oligomerize [32].…”

Section: Figure 4 Designing the Self-assembly Of Repeat Proteinsmentioning

confidence: 99%

“…Exploiting these properties, one can extend the modular design process from individual repeat proteins to the assembly of repeat proteins into novel biomaterials with encoded properties and precisely displayed functional sites. To date, examples of this exciting field includes using metals, peptide binding, native chemical ligation and disulfide bonding to assemble repeat proteins into gels, films and fibres (Figure 4) [26][27][28]. One interesting design aspect that is peculiar to linear repeat proteins is the potential to change the shape of the super-helix (curvature, twist, pitch).…”

Section: Future Directions: Repeat-protein Design and Assemblymentioning

confidence: 99%

Dissecting and reprogramming the folding and assembly of tandem-repeat proteins

Rowling

Sivertsson

Perez-Riba

et al. 2015

Biochemical Society Transactions

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Studying protein folding and protein design in globular proteins presents significant challenges because of the two related features, topological complexity and co-operativity. In contrast, tandem-repeat proteins have regular and modular structures composed of linearly arrayed motifs. This means that the biophysics of even giant repeat proteins is highly amenable to dissection and to rational design. Here we discuss what has been learnt about the folding mechanisms of tandem-repeat proteins. The defining features that have emerged are: (i) accessibility of multiple distinct routes between denatured and native states, both at equilibrium and under kinetic conditions; (ii) different routes are favoured for folding compared with unfolding; (iii) unfolding energy barriers are broad, reflecting stepwise unravelling of an array repeat by repeat; (iv) highly co-operative unfolding at equilibrium and the potential for exceptionally high thermodynamic stabilities by introducing consensus residues; (v) under force, helical-repeat structures are very weak with non-co-operative unfolding leading to elasticity and buffering effects. This level of understanding should enable us to create repeat proteins with made-to-measure folding mechanisms, in which one can dial into the sequence the order of repeat folding, number of pathways taken, step size (co-operativity) and fine-structure of the kinetic energy barriers.

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“…The length (and thus mass) is controlled by the number of repeat motifs used. 29 A whole library of repeat proteins has been developed by Plückthun and coworkers. Their designed ankyrin repeat proteins (DARPins) con-sist of ankyrin repeat modules with different numbers of repeats and end caps on the C-and the N-terminus.…”

Section: Introductionmentioning

confidence: 99%

A New, Modular Mass Calibrant for High-Mass MALDI-MS

et al. 2013

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The application of matrix-assisted laser desorption/ionization mass spectrometry (MALDIMS) for the analysis of high-mass proteins requires suitable calibration standards at high m/z ratios. Several possible candidates were investigated, and concatenated polyproteins based on recombinantly expressed maltodextrin-binding protein (MBP) are shown here to be well suited for this purpose. Introduction of two specific recognition sites into the primary sequence of the polyprotein allows for the selective cleavage of MBP3 into MBP and MBP2. Moreover, these MBP2 and MBP3 oligomers can be dimerized specifically, such that generation of MPB4 and MBP6 is possible as well. With the set of calibrants presented here, the m/z range of 40-400 kDa is covered. Since all calibrants consist of the same species and differ only in mass, the ionization efficiency is expected to be similar. However, equimolar mixtures of these proteins did not yield equal signal intensities on a detector specifically designed for detecting high-mass molecules. and MBP 6 is possible as well. With the set of calibrants presented here, the m/z range of 40-400 kDa is covered. Since all calibrants consist of the same species and differ only in mass, the ionization efficiency is expected to be similar. However, equimolar mixtures of these proteins did not yield equal signal intensities on a detector specifically designed for detecting high-mass molecules.

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

Cited by 35 publications

References 35 publications

Biomolecular templating of functional hybrid nanostructures using repeat protein scaffolds

Biomolecular templating of functional hybrid nanostructures using repeat protein scaffolds

Dissecting and reprogramming the folding and assembly of tandem-repeat proteins

A New, Modular Mass Calibrant for High-Mass MALDI-MS

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