Structure of single-wall peptide nanotubes: in situ flow aligning X-ray diffraction

Castelletto, Valeria; Nutt, David; Hamley, Ian W.; Bucak, Şeyda; Cenker, Çelen Çağrı; Olsson, Ulf

doi:10.1039/c0cc00212g

Cited by 64 publications

(87 citation statements)

References 23 publications

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“…Because of the very large aspect ratio, the tubes form an ordered phase that presumably is nematic, suggesting the favorable self-assembly of antiparallel peptide dimers into β-sheet ribbons that wrap helically to form the nanotube wall. 31,32 Moreover, similar to the dynamic behavior of phospholipid vesicles and other microstructures, 33 these simplest of peptide nanostructures appear to behave as dynamic entities in water;they fuse, divide, and change shape as a function of time and environmental influence (Figures 4À6). 23À30…”

Section: Simple Amino Acids and Their Condensation Under Prebiotic Comentioning

confidence: 95%

Lipid-like Self-Assembling Peptides

Zhang

2012

Acc. Chem. Res.

121

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One important question in prebiotic chemistry is the search for simple structures that might have enclosed biological molecules in a cell-like space. Phospholipids, the components of biological membranes, are highly complex. Instead, we looked for molecules that might have been available on prebiotic Earth. Simple peptides with hydrophobic tails and hydrophilic heads that are made up of merely a combination of these robust, abiotically synthesized amino acids and could self-assemble into nanotubes or nanovesicles fulfilled our initial requirements. These molecules could provide a primitive enclosure for the earliest enzymes based on either RNA or peptides and other molecular structures with a variety of functions. We discovered and designed a class of these simple lipid-like peptides, which we describe in this Account. These peptides consist of natural amino acids (glycine, alanine, valine, isoleucine, leucine, aspartic acid, glutamic acid, lysine, and arginine) and exhibit lipid-like dynamic behaviors. These structures further undergo spontaneous assembly to form ordered arrangements including micelles, nanovesicles, and nanotubes with visible openings. Because of their simplicity and stability in water, such assemblies could provide examples of prebiotic molecular evolution that may predate the RNA world. These short and simple peptides have the potential to self-organize to form simple enclosures that stabilize other fragile molecules, to bring low concentration molecules into a local environment, and to enhance higher local concentration. As a result, these structures plausibly could not only accelerate the dehydration process for new chemical bond formation but also facilitate further self-organization and prebiotic evolution in a dynamic manner. We also expect that this class of lipid-like peptides will likely find a wide range of uses in the real world. Because of their favorable interactions with lipids, these lipid-like peptides have been used to solubilize and stabilize membrane proteins, both for scientific studies and for the fabrication of nanobiotechological devices. They can also increase the solubility of other water-insoluble molecules and increase long-term stability of some water-soluble proteins. Likewise, because of their lipophilicity, these structures can deliver molecular cargo, such as small molecules, siRNA, and DNA, in vivo for potential therapeutic applications.

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Section: Simple Amino Acids and Their Condensation Under Prebiotic Comentioning

confidence: 95%

Lipid-like Self-Assembling Peptides

Zhang

2012

Acc. Chem. Res.

121

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“…The self-assembly of AnK is concentration dependent. A6K was found to self-assemble above a critical concentration in aqueous solutions and form hollow nanotubes with a radius of 26 nm (Figure 2C), followed by a transition to a nematic lamellar phase with increasing peptide concentration (Bucak et al, 2009;Castelletto et al, 2010;Cenker et al, 2011). A4K could not self-assemble to form nanostructures.…”

Section: Small Surfactant-like Peptide Based On the Silk Protein Domainmentioning

confidence: 99%

Development of New Smart Materials and Spinning Systems Inspired by Natural Silks and Their Applications

Cheng

Lee

2016

Front. Mater.

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Silks produced by spiders and silkworms are charming natural biological materials with highly optimized hierarchical structures and outstanding physicomechanical properties. The superior performance of silks relies on the integration of a unique protein sequence, a distinctive spinning process, and complex hierarchical structures. Silks have been prepared to form a variety of morphologies and are widely used in diverse applications, for example, in the textile industry, as drug delivery vehicles, and as tissue engineering scaffolds. This review presents an overview of the organization of natural silks, in which chemical and physical functions are optimized, as well as a range of new materials inspired by the desire to mimic natural silk structure and synthesis.

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“…[18][19][20][21] Parallel a-sheet has also been suggested as the structure adopted initially during amyloid formation. [22][23][24][25][26][27] b-sheets formed by amyloid proteins are widely considered to gain their exceptional stability by folding into helical nanotube structures [28][29][30][31][32][33][34][35][36][37][38][39][40] of varying dimensions. Many amyloid fibrils have been shown to have a cross-b structure; that is, the b-strands run perpendicular to the fibril axis.…”

mentioning

confidence: 99%

Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments

Hayward

Milner‐White

2017

Proteins

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Examples of homomeric β-helices and β-barrels have recently emerged. Here we generalise the theory for the shear number in β-barrels to encompass β-helices and homomeric structures. We introduce the concept of the "β-strip", the set of parallel or antiparallel neighbouring strands, from which the whole helix can be generated giving it n-fold rotational symmetry. In this context the shear number is interpreted as the sum around the helix of the fixed register shift between neighbouring identical β-strips. Using this approach we have derived relationships between helical width, pitch, angle between strand direction and helical axis, mass per length, register shift, and number of strands. The validity and unifying power of the method is demonstrated with known structures including α-haemolysin, T4 phage spike, cylindrin, and the HET-s(218-289) prion. From reported dimensions measured by Xray fibre diffraction on amyloid fibrils the relationships can be used to predict the register shift and the number of strands within amyloid protofilaments. This was used to construct models of transthyretin and Alzheimer β(40) amyloid protofilaments that comprise a single strip of in-register β-strands folded into a "β-strip helix". Results suggest both stabilisation of an individual β-strip helix as well as growth by addition of further β-strip helices involves the same pair of sequence segments associating with β-sheet hydrogen bonding at the same register shift. This association would be aided by a repeat sequence. Hence understanding of how the register shift (as the distance between repeat sequences) relates to helical dimensions, will be useful for nanotube design.

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Structure of single-wall peptide nanotubes: in situ flow aligning X-ray diffraction

Cited by 64 publications

References 23 publications

Lipid-like Self-Assembling Peptides

Lipid-like Self-Assembling Peptides

Development of New Smart Materials and Spinning Systems Inspired by Natural Silks and Their Applications

Geometrical principles of homomeric β-barrels and β-helices: Application to modeling amyloid protofilaments

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