Self-Assembly Process of Peptide Amphiphile Worm-Like Micelles

Shimada, Toshio; Sakamoto, Naoki; Motokawa, Ryuhei; Koizumi, Satoshi; Tirrell, Matthew

doi:10.1021/jp209105z

Cited by 55 publications

(56 citation statements)

References 19 publications

(27 reference statements)

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“…While PA fibres with high concentration are known to bundle themselves and form close packed hexagonal network36, we demonstrate that water molecules between fibres in these close packed hexagon play a key role in stabilizing this fibre network. Note that the process of micelle formation followed by fibre formation has been reported in previous experimental and simulation studies133738394041. Previously Tirrell et al .…”

Section: Resultssupporting

confidence: 56%

“…The cryo-TEM images of the C16−W3K solution taken immediately after making the solution showed existence of many discrete spherical micelle structures of around 10 nm diameter39. They also found spherical and shorter ‘worm-like' micelles which suggested that micellar transition occurs through collision of spherical micelles and/or shorter extended micelles; at least during the initial stages40. AFM images by Shimada et al .…”

Section: Resultsmentioning

confidence: 96%

“…Previously Tirrell et al . have investigated self-assembly of C16−W3K PA by using a suite of different experimental methods including cryogenic transmission electron microscopy (cryo-TEM), rheological measurement, circular dichroism, and atomic force microscopy (AFM) and infrared (IR) spectroscopy in the attenuated total reflection mode3940. The cryo-TEM images of the C16−W3K solution taken immediately after making the solution showed existence of many discrete spherical micelle structures of around 10 nm diameter39.…”

Section: Resultsmentioning

confidence: 99%

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Water ordering controls the dynamic equilibrium of micelle–fibre formation in self-assembly of peptide amphiphiles

et al. 2016

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Understanding the role of water in governing the kinetics of the self-assembly processes of amphiphilic peptides remains elusive. Here, we use a multistage atomistic-coarse-grained approach, complemented by circular dichroism/infrared spectroscopy and dynamic light scattering experiments to highlight the dual nature of water in driving the self-assembly of peptide amphiphiles (PAs). We show computationally that water cage formation and breakage near the hydrophobic groups control the fusion dynamics and aggregation of PAs in the micellar stage. Simulations also suggest that enhanced structural ordering of vicinal water near the hydrophilic amino acids shifts the equilibrium towards the fibre phase and stimulates structure and order during the PA assembly into nanofibres. Experiments validate our simulation findings; the measured infrared O–H bond stretching frequency is reminiscent of an ice-like bond which suggests that the solvated water becomes increasingly ordered with time in the assembled peptide network, thus shedding light on the role of water in a self-assembly process.

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Section: Resultssupporting

confidence: 56%

Section: Resultsmentioning

confidence: 96%

Section: Resultsmentioning

confidence: 99%

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Water ordering controls the dynamic equilibrium of micelle–fibre formation in self-assembly of peptide amphiphiles

et al. 2016

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“…When the peptide was coupled to short alkyl chains (containing 12 or less carbons) no aggregates were formed, whereas with longer tails (containing more than 16 carbons) the PAs formed highly stable assemblies. Tirrell and co‐workers have investigated PA molecules that can self‐assemble into micellar structures . A different PA design, containing a pentapeptide head group based on a sequence from procollagen I attached to a hexadecyl lipid chain (C 16 ‐KT 2 KS) was shown to assemble into extended nanotapes in aqueous solution .…”

Section: Design Of Supramolecular Materialsmentioning

confidence: 99%

Self‐assembly in nature: using the principles of nature to create complex nanobiomaterials

Mendes

Baran

Reis

et al. 2013

WIREs Nanomed Nanobiotechnol

350

351

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Self-assembly is a ubiquitous process in biology where it plays numerous important roles and underlies the formation of a wide variety of complex biological structures. Over the past two decades, materials scientists have aspired to exploit nature's assembly principles to create artificial materials, with hierarchical structures and tailored properties, for the fabrication of functional devices. Toward this goal, both biological and synthetic building blocks have been subject of extensive research in self-assembly. In fact, molecular self-assembly is becoming increasingly important for the fabrication of biomaterials because it offers a great platform for constructing materials with high level of precision and complexity, integrating order and dynamics, to achieve functions such as stimuli-responsiveness, adaptation, recognition, transport, and catalysis. The importance of peptide self-assembling building blocks has been recognized in the last years, as demonstrated by the literature available on the topic. The simple structure of peptides, as well as their facile synthesis, makes peptides an excellent family of structural units for the bottom-up fabrication of complex nanobiomaterials. Additionally, peptides offer a great diversity of biochemical (specificity, intrinsic bioactivity, biodegradability) and physical (small size, conformation) properties to form self-assembled structures with different molecular configurations. The motivation of this review is to provide an overview on the design principles for peptide self-assembly and to illustrate how these principles have been applied to manipulate their self-assembly across the scales. Applications of self-assembling peptides as nanobiomaterials, including carriers for drug delivery, hydrogels for cell culture and tissue repair are also described.

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“…Phe-Phe, tert-butyl dicarbonate (Boc)-Phe-Phe) 7,8,[16][17][18][19][20][21] . The structures formed by these homoaromatic peptides include tubular structures, spheres, sheet-like assemblies and fibers 6,8,15,[21][22][23][24][25][26][27][28][29][30][31][32] . The fibers in some cases generate a fibril mesh that yields a hydrogel [33][34][35][36][37] .…”

Section: Introductionmentioning

confidence: 99%

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Yuran

Reches

2013

JoVE

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In nature, complex functional structures are formed by the self-assembly of biomolecules under mild conditions. Understanding the forces that control self-assembly and mimicking this process in vitro will bring about major advances in the areas of materials science and nanotechnology. Among the available biological building blocks, peptides have several advantages as they present substantial diversity, their synthesis in large scale is straightforward, and they can easily be modified with biological and chemical entities 1,2 . Several classes of designed peptides such as cyclic peptides, amphiphile peptides and peptide-conjugates self-assemble into ordered structures in solution. Homoaromatic dipeptides, are a class of short self-assembled peptides that contain all the molecular information needed to form ordered structures such as nanotubes, spheres and fibrils [3][4][5][6][7][8] . A large variety of these peptides is commercially available. This paper presents a procedure that leads to the formation of ordered structures by the self-assembly of homoaromatic peptides. The protocol requires only commercial reagents and basic laboratory equipment. In addition, the paper describes some of the methods available for the characterization of peptide-based assemblies. These methods include electron and atomic force microscopy and Fourier-Transform Infrared Spectroscopy (FT-IR). Moreover, the manuscript demonstrates the blending of peptides (coassembly) and the formation of a "beads on a string"-like structure by this process. 9 The protocols presented here can be adapted to other classes of peptides or biological building blocks and can potentially lead to the discovery of new peptide-based structures and to better control of their assembly. Video LinkThe video component of this article can be found at

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Self-Assembly Process of Peptide Amphiphile Worm-Like Micelles

Cited by 55 publications

References 19 publications

Water ordering controls the dynamic equilibrium of micelle–fibre formation in self-assembly of peptide amphiphiles

Water ordering controls the dynamic equilibrium of micelle–fibre formation in self-assembly of peptide amphiphiles

Self‐assembly in nature: using the principles of nature to create complex nanobiomaterials

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

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