Self‐Assembling Nanostructures from Coiled‐Coil Peptides

Ryadnov, Maxim G.; Woolfson, Derek N.

doi:10.1002/9783527610389.ch2

Cited by 11 publications

(2 citation statements)

References 57 publications

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“…The coiled coil motif is another protein structure that has been exploited in the design of self-assembled, supramolecular peptide materials. 480–483 The α -helical secondary structure consists of seven-amino acid repeats that compromise two turns of the standard helix, with each amino acid in this heptad denoted as abcdefg (Figure 31A). Coiled coils are bundles of two to seven α -helices stabilized by hydrophobic knob-in-hole and complementary electrostatic interactions between the constituent α -helices.…”

Section: Coiled-coil Peptidesmentioning

confidence: 99%

Multicomponent peptide assemblies

2018

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Self-assembled peptide nanostructures have been increasingly exploited as functional materials for applications in biomedicine and energy. The emergent properties of these nanomaterials determine the applications for which they can be exploited. It has recently been appreciated that nanomaterials composed of multicomponent coassembled peptides often display unique emergent properties that have the potential to dramatically expand the functional utility of peptide-based materials. This review presents recent efforts in the development of multicomponent peptide assemblies. The discussion includes multicomponent assemblies derived from short low molecular weight peptides, peptide amphiphiles, coiled coil peptides, collagen, and β-sheet peptides. The design, structure, emergent properties, and applications for these multicomponent assemblies are presented in order to illustrate the potential of these formulations as sophisticated next-generation bio-inspired materials.

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Section: Coiled-coil Peptidesmentioning

confidence: 99%

Multicomponent peptide assemblies

2018

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“…Several de novo design principals were adopted for long peptide sequences contained 20 or more amino acids to fold into helical conformation and self-assembled into tailored functional materials. The α-helix based coiled-coil protein structure has been extensively exploited in the design of self-assembled, one-dimensional nanofibrous materials [ 24 , 25 ]. The most common strategy is design based on the “sticky-end” concept in which α-helical peptides interact, leaving dangling ends that can nucleate the addition of further helices at both ends and support growth in axial direction.…”

Section: Nanostructures Of Helical Peptides For Diverse Functional Apmentioning

confidence: 99%

Self-assembly of Functional Nanostructures by Short Helical Peptide Building Blocks

Bera

Gazit

2019

PPL

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The self-assembly of short peptide building blocks into well-ordered nanostructures is a key direction in bionanotechnology. The formation of β -sheet organizations by short peptides is well explored, leading to the development of a wide range of functional assemblies. Likewise, many natural proteinaceous materials, such as silk and amyloid fibrils, are based on β-sheet structures. In contrast, collagen, the most abundant protein in mammals, is based on helical arrangement. Similar to β-sheet structures, short helical peptides have been recently discovered to possess a diverse set of functionalities with the potential to fabricate artificial self-assembling materials. Here, we outline the functional roles of self-assembled nanostructures formed by short helical peptides and their potential as artificial materials. We focus on the association between self-assembled mesoscale structures and their material function and demonstrate the way by which this class of building blocks bears the potential for diverse applications, such as the future fabrication of smart devices.

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Self‐Assembly of One‐ and Two‐Dimensional Hemoprotein Systems by Polymerization through Heme–Heme Pocket Interactions

et al. 2009

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Supramolekulare Proteinpolymere: Wenn eine Hämeinheit an der Oberfläche einer Apo‐Cytochrom‐b562(H63C)‐Mutante eingeführt wird, entstehen durch nichtkovalente Wechselwirkungen zwischen Hämtaschen supramolekulare Polymere. Der Einbau einer Hämtriade als Angelmolekül in das Proteinpolymer führt zu einer zweidimensionalen Proteinnetzwerkstruktur, die mithilfe der Rasterkraftmikroskopie im intermittierenden Modus sichtbar gemacht wurde (siehe Bild).

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Self‐Assembling Nanostructures from Coiled‐Coil Peptides

Cited by 11 publications

References 57 publications

Multicomponent peptide assemblies

Multicomponent peptide assemblies

Self-assembly of Functional Nanostructures by Short Helical Peptide Building Blocks

Self‐Assembly of One‐ and Two‐Dimensional Hemoprotein Systems by Polymerization through Heme–Heme Pocket Interactions

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