2016
DOI: 10.1039/c6sc01306f
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Repeat protein scaffolds: ordering photo- and electroactive molecules in solution and solid state

Abstract: An innovative approach is investigated in which a protein building block is designed to organize porphyrin molecules. The strategy is based on a modular protein unit with tunable properties including stability, function and self-assembly.

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Cited by 30 publications
(33 citation statements)
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“…In a previous work, we presented a novel bioinspired approach in which photoactive porphyrin derivatives were covalently connected to the helical scaffold of a designed repeat protein, in particular a consensus tetratricopeptide repeat (CTPR) protein, giving rise to an ordered and oriented bioorganic conjugate . Specifically, a mutated CTPR protein with four repeated units was designed, introducing two cysteine residues in each repeat to provide unique reactivity for the immobilization of the porphyrin derivatives.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…In a previous work, we presented a novel bioinspired approach in which photoactive porphyrin derivatives were covalently connected to the helical scaffold of a designed repeat protein, in particular a consensus tetratricopeptide repeat (CTPR) protein, giving rise to an ordered and oriented bioorganic conjugate . Specifically, a mutated CTPR protein with four repeated units was designed, introducing two cysteine residues in each repeat to provide unique reactivity for the immobilization of the porphyrin derivatives.…”
Section: Introductionmentioning
confidence: 99%
“…Specifically, a mutated CTPR protein with four repeated units was designed, introducing two cysteine residues in each repeat to provide unique reactivity for the immobilization of the porphyrin derivatives. The hybrid conjugates retained the structure and assembly properties of the protein scaffold and displayed the spectroscopic features of orderly aggregated porphyrins along the protein structure . Herein, we present the creation of novel protein–SWCNT donor–acceptor bio‐nanohybrids from our recent bioinspired approach with potential applications in the so‐called “biomolecular electronics.”…”
Section: Introductionmentioning
confidence: 99%
“…Indeed, the possible applications of such materials are extremely diverse: from nanoscale switches and sensors that respond to, for instance, temperature, light or pH, to catalysts (mimicking the spatially defined catalysis of proteins) [179][180][181] and materials with three-dimensional connectivity that can be used, e.g., to optimize charge separation in photovoltaics. 182,183 In order to reproduce the protein folding process at the nano-and micro-scale level, patchy particles can prove themselves essential: anisotropically interacting units arranged in strings could play the same role as the residues constituting the proteins, effectively constructing functionalized colloidal chains, the so-called ''patchy polymers'' [184][185][186] (see panel (a) of Fig. 4).…”
Section: Patchy Polymersmentioning
confidence: 99%
“…CTPRs have a modular structure, in which the repeats can be combined in tandem to form highly stable CTPR proteins that display a right‐handed superhelical structure, with eight repeats per full turn of the superhelix . These features make these repeat protein scaffolds ideal building blocks for numerous applications, as previously demonstrated through the fabrication of functional protein‐based materials . Similarly, we hypothesize that materials based on CTPR proteins will be applicable for the ordered entrapment and immobilization of enzymes toward the generation of novel heterogeneous biocatalysts that can be readily integrated into devices.…”
Section: Introductionmentioning
confidence: 99%