Nanolithography: Small 8/2010

Han, Tae Hee; Ok, Taedong; Kim, Jangbae; Shin, Dong Ok; Ihee, Hyotcherl; Lee, Hee-Seung; Kim, Sang Ouk

doi:10.1002/smll.201090023

Cited by 9 publications

(11 citation statements)

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“…Transmission electron microscopy and spectroscopy studies reported that Boc-FFF (an analogy of FFF) can assemble into solid nanospheres. 41 Fusion of small clusters into nanospheres/nanorods is observed in the self-assembly trajectory of 600/1800 FF/FFF peptides. We propose that the formation of large-scale FF/FFF assemblies observed experimentally might take place through multiple fusion processes of small Table 3 Total potential energy (E total ) and potential energy components of FFF and FF nanostructures.…”

Section: Resultsmentioning

confidence: 99%

“…the N-terminus is protected with a t-butyloxycarbonyl (Boc) group and the C-terminus is a free carboxylic acid) can assemble into nanospheres which were fully lled without void space. 41 On the computational side, Tamamis et al investigated the selfassembly of 12 FF or 8 FFF peptide chains using replicaexchange MD simulations with an implicit solvent. 40 They found that both FFF and FF peptides can form aggregates containing open or ring-like peptide networks, with FFF peptides displaying a higher network-forming propensity than FF.…”

Section: Introductionmentioning

confidence: 99%

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Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides

et al. 2014

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Understanding the nature of the self-assembly of peptide nanostructures at the molecular level is critical for rational design of functional bio-nanomaterials. Recent experimental studies have shown that triphenylalanine(FFF)-based peptides can self-assemble into solid plate-like nanostructures and nanospheres, which are different from the hollow nanovesicles and nanotubes formed by diphenylalanine(FF)-based peptides. In spite of extensive studies, the assembly mechanism and the molecular basis for the structural differences between FFF and FF nanostructures remain poorly understood. In this work, we first investigate the assembly process and the structural features of FFF nanostructures using coarse-grained molecular dynamics simulations, and then compare them with FF nanostructures. We find that FFF peptides spontaneously assemble into solid nanometer-sized nanospheres and nanorods with substantial β-sheet contents, consistent with the structural properties of hundred-nanometer-sized FFF nano-plates characterized by FT-IR spectroscopy. Distinct from the formation mechanism of water-filled FF nanovesicles and nanotubes reported in our previous study, intermediate bilayers are not observed during the self-assembly process of FFF nanospheres and nanorods. The peptides in FFF nanostructures are predominantly anti-parallel-aligned, which can form larger sizes of β-sheet-like structures than the FF counterparts. In contrast, FF peptides exhibit lipid-like assembly behavior and assemble into bilayered nanostructures. Furthermore, although the self-assembly of FF and FFF peptides is mostly driven by side chain-side chain (SC-SC) aromatic stacking interactions, the main chain-main chain (MC-MC) interactions also play an important role in the formation of fine structures of the assemblies. The delicate interplay between MC-MC and SC-SC interactions results in the different nanostructures formed by the two peptides. These findings provide new insights into the structure and self-assembly pathway of di-/tri-phenylalanine peptide assemblies, which might be helpful for the design of bioinspired nanostructures.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides

et al. 2014

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“…2−6 Driven by cooperative noncovalent interactions such as hydrogen bonding, hydrophobic forces, electrostatic interactions, π−π stacking, and nonspecific van der Waals forces, peptides can spontaneously form well-defined nanostructures. 7 Self-assembled peptides exhibit a range of structural architectures including nanorods, 8 -tubes, 9,10 -fibers, 11,12 -spheres, 13,14 and -donuts 15 as well as conventional micelles. 16 These nanostructures have been widely used as structural scaffoldings, selective transport channels, and templates for mineral formation.…”

Section: ■ Introductionmentioning

confidence: 99%

Morphology Transformation via pH-Triggered Self-Assembly of Peptides

Qin

Zhuo

et al. 2011

Langmuir

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Three flexible peptides (P1: (C(17)H(35)CO-NH-GRGDG)(2)KG; P2: (Fmoc-GRGDG)(2)KG; P3: (CH(3)CO-NH-GRGDG)(2)KG) self-assembled to form a variety of morphologically distinct assemblies at different pHs. P1 formed nanofibers at pH 3, then self-assembled into nanospheres with pH up to 6 and further changed to lamellar structures when the pH value was further increased to 10. P2 aggregated into an entwined network structure at pH 3, and then self-assembled into well-defined nanospheres, lamellar structures, and vesicles via adjusting the pH value. However, P3 did not self-assemble into well-ordered nanostructures, presumably due to the absence of a large hydrophobic group. The varying self-assembly behaviors of the peptides at different pHs are attributed to molecular conformational changes. These self-assembled supramolecular materials might contribute to the development of new peptide-based biomaterials.

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“…Self-assembled structural transitions induced by solvent, 21 addition of new reagents, 22,23 and environmental stimuli [24][25][26] were interestedly studied. Hierarchical self-assembly, referring to self-assembly step by step with multiple levels, was involved in biologically normal and abnormal processes, and utilized to fabricate nanoarchitectures mimicking viral capsids, 27 bionanospheres for lithography, 28 hexagonal peptide microtubes for optical waveguiding, 29 and other nanostructures. 30 Although many methodologies were developed to modulate the hierarchical self-assembly of peptides, the internal or environmental factors affecting the self-assembly procedure and resulting in the neurodegenerative diseases were oen ignored.…”

Section: Introductionmentioning

confidence: 99%

Hierarchical self-assembly of a β-amyloid peptide derivative

et al. 2013

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Neurodegenerative diseases including Alzheimer's, Parkinson's, and type II diabetes are recognized to be related to proteins misfolding into amyloid fibrils and other aggregates with a b-sheet conformation.Herein, self-assembled peptide micro/nanoarchitectures were designed and prepared to mimic those aggregates. A short b-amyloid peptide derivative with a diphenylalanine moiety was synthesized, which could self-assemble into nanofibers via b-sheet conformation in an aqueous solution with a concentration of 1 mg mL À1 at pH about 8. By adjusting the pH to around 6.5, a peptide solution with a concentration of 15 mg mL À1 could change to a supramolecular hydrogel. The influence of selfassembly conditions including peptide concentration, temperature, pressure, and self-assembly time were investigated in detail. It was found that the self-assembled nanofibers could further aggregate into catenulate microfibers in solution as well as layer-by-layer plaques in the hydrogel under particular conditions.

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Nanolithography: Small 8/2010

Cited by 9 publications

References 0 publications

Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides

Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides

Morphology Transformation via pH-Triggered Self-Assembly of Peptides

Hierarchical self-assembly of a β-amyloid peptide derivative

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