Template-Directed Assembly of a <i>de Novo </i>Designed Protein

Brown, Christina L.; Aksay, İlhan A.; Saville, D. A.; Hecht, Michael H.

doi:10.1021/ja0261271

Cited by 105 publications

(122 citation statements)

References 15 publications

(25 reference statements)

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“…Previously, protein films have been generated from b-strand amyloid fibres of proteins [5,34]. In addition, coil-coiled fibreforming peptides were also successfully rationally engineered to generate nanostructured fibrous materials [6].…”

Section: Discussionmentioning

confidence: 99%

Nanostructured functional films from engineered repeat proteins

Grove

Regan

Cortajarena

2013

J. R. Soc. Interface.

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Fundamental advances in biotechnology, medicine, environment, electronics and energy require methods for precise control of spatial organization at the nanoscale. Assemblies that rely on highly specific biomolecular interactions are an attractive approach to form materials that display novel and useful properties. Here, we report on assembly of films from the designed, rod-shaped, superhelical, consensus tetratricopeptide repeat protein (CTPR). We have designed three peptide-binding sites into the 18 repeat CTPR to allow for further specific and non-covalent functionalization of films through binding of fluorescein labelled peptides. The fluorescence signal from the peptide ligand bound to the protein in the solid film is anisotropic, demonstrating that CTPR films can impose order on otherwise isotropic moieties. Circular dichroism measurements show that the individual protein molecules retain their secondary structure in the film, and X-ray scattering, birefringence and atomic force microscopy experiments confirm macroscopic alignment of CTPR molecules within the film. This work opens the door to the generation of innovative biomaterials with tailored structure and function.

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Section: Discussionmentioning

confidence: 99%

Nanostructured functional films from engineered repeat proteins

Grove

Regan

Cortajarena

2013

J. R. Soc. Interface.

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“…[2][3][4] Conversely, inorganic substrates may act as templates to induce large-scale order in protein supramolecular structures. [5,6] An understanding of these processes requires insight into the fundamental nature of the interactions between proteins and inorganic substrates. To this end we have carried out an empirical study of the adsorption and self-assembly behavior of a model peptide, CH 3 CO-Q-Q-R-F-Q-W-Q-F-E-Q-Q-CONH 2 (P 11 -2), [8] at solution/mica interfaces, and find that tapes with a cross b-sheet structure, a single molecule in thickness, grow epitaxially to produce a two-dimensional network reflecting the hexagonal symmetry of the substrate.…”

mentioning

confidence: 99%

Adsorption and Self‐Assembly of Peptides on Mica Substrates

et al. 2005

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“…[9][10][11][12][13] Particularly, onedimensional growth of peptides or proteins on inorganic substrates has been recognized as a potential approach to the fabrication of functional nanostructures. [14][15][16] In these cases the peptide (or protein) is precisely assembled with the assistance of inorganic templates. [7,8] This feature allows the arrangement of peptide molecules in a predesignated orientation on substrates by proper design of the peptide sequences.…”

mentioning

confidence: 99%

“…The combination of the above results strongly supports an upright orientation. On the HOPG surface, the height and deconvoluted width [16,25] of GAV-9 tapes are 0.9 AE 0.1 nm and 3-4 nm, respectively. They are approximately equal to the dimensions of GAV-9 (1.0 nm in diameter, 3.1 nm in length).…”

mentioning

confidence: 99%

Epitaxial Growth of Peptide Nanofilaments on Inorganic Surfaces: Effects of Interfacial Hydrophobicity/Hydrophilicity

Zhang

et al. 2006

Angew Chem Int Ed

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The self-assembly of peptides and proteins has recently attracted much attention because of its scientific importance and widespread applications in the fields of nanomaterials, [1][2][3][4][5] crystallography, [6][7][8] and pathology. [9][10][11][12][13] Particularly, onedimensional growth of peptides or proteins on inorganic substrates has been recognized as a potential approach to the fabrication of functional nanostructures. [14][15][16] In these cases the peptide (or protein) is precisely assembled with the assistance of inorganic templates. [7,8] This feature allows the arrangement of peptide molecules in a predesignated orientation on substrates by proper design of the peptide sequences.Previous studies showed that different substrates have significant effects on the formation of nanofilaments. [17][18][19][20] As it is generally accepted that the hydrophobic interaction between the side chains is a driving force in the formation of peptide nanofilaments, it is very important to explore the effects of the substrate hydrophobicity/hydrophilicity on the relevant template-assisted epitaxial growth, which has not been systematically studied so far.Herein, we compare the self-assembly behavior of the peptide GAV-9 on hydrophilic mica and hydrophobic HOPG (highly ordered pyrolytic graphite) surfaces by in situ atomic force microscopy (AFM) to investigate how interfacial hydrophobicity/hydrophilicity influences the epitaxial growth of peptide nanofilaments.GAV-9, NH 2 -VGGAVVAGV-CONH 2 (Figure 1 a), consists of hydrophobic amino acid residues and is a conserved consensus of three neurodegenerative-disease-related proteins: a-synuclein, amyloid b protein, and prion protein, which are capable of forming amyloid fibrils in vivo and in vitro. [20][21][22] Unlike a-synuclein, GAV-9 with a concentration of 1.6 mm or less cannot form amyloid fibrils even when its solution is incubated under fibrillization-accelerating conditions [21] for a long time ( % 6 days), as characterized by AFM and turbidity measurements (data not shown). Circular dichroism experiments show that GAV-9 in fresh solutions adopts a random-coil structure, but forms b-sheets when dried (Supporting Information).However, AFM studies indicate that GAV-9 forms uniform nanofilaments from random-coil monomeric solutions through template-assisted growth on surfaces, including tapelike objects [19] on HOPG and fibrillike aggregates [23] on mica (Figure 2). Both the tapes and fibrils grow epitaxially across the surface and show three preferred orientations at 1208 to each other. The Fourier transform confirms its threefold symmetry (inset of Figure 2 b and Figure 2 e). It was also found that orientations of the tapes and the fibrils are consistent with the underlying atomic lattice of the substrates (Figure 2 a and Figure 2 b, Supporting Information). These results indicate that the self-assembly of GAV-9 is a onedimensional epitaxial growth process, similar to those previously reported. [14][15][16][17] Solid-state ATR (attenuated total reflectance) IR spect...

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Template-Directed Assembly of a de Novo Designed Protein

Cited by 105 publications

References 15 publications

Nanostructured functional films from engineered repeat proteins

Nanostructured functional films from engineered repeat proteins

Adsorption and Self‐Assembly of Peptides on Mica Substrates

Epitaxial Growth of Peptide Nanofilaments on Inorganic Surfaces: Effects of Interfacial Hydrophobicity/Hydrophilicity

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