Bionanosphere Lithography via Hierarchical Peptide Self‐Assembly of Aromatic Triphenylalanine

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

doi:10.1002/smll.200902050

Cited by 63 publications

(61 citation statements)

References 45 publications

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“…19,20 More specifically, FFF and Fmoc-4 structural defects in FFFF tubes are due to the fact that the increment in the conformational flexibility is accompanied by a reduction in the number of restrictions associated with hydrogen bonds. In opposition, Fmoc-FFFF organizes into a variety of polymorphs depending on the experimental conditions, which included ultra-thin nanoplates, fibrils and star-like submicrometric aggregates.…”

Section: Introductionmentioning

confidence: 99%

Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites

et al. 2016

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Homopeptides with 2, 3 and 4 phenylalanine (Phe) residues and capped with fluorenylmethoxycarbonyl and fluorenylmethyl ester at the N-and C-terminus, respectively, have been synthesized to examine their self-assembly capabilities.Depending on the conditions, the di-and triphenylalanine derivatives self-organize into a wide variety of stable polymorphic structures, which have been characterized: stacked braids, doughnuts-like, bundled arrays of nanotubes, corkscrew-like and spherulitic microstructures. These highly aromatic Phe-based peptides also form incipient branched dendritic microstructures, even though they are highly unstable, making their manipulation very difficult. In opposition, the tetraphenylalanine derivative spontaneously self-assemble into stable dendritic microarchitectures made of branches growing from nucleated primary frameworks. The fractal dimension of these microstructures is 1.70, which evidences self-similarity and two-dimensional diffusion controlled growth. DFT calculations at the M06L/6-31G(d) level have been carried out on model -sheets since it is the most elementary building block of Phe-based peptide polymorphs. Results indicate that the antiparallel -sheet is more stable than the parallel one, the difference between them growing with the number of Phe residues. Thus, the cooperative effects associated with the antiparallel disposition become more favorable when the number of Phe residues increases from 2 to 4, while those of the parallel disposition remained practically constant.3

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Section: Introductionmentioning

confidence: 99%

Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites

et al. 2016

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“…

Nature utilizes the self-assembly of monomeric units by multiple noncovalent interactions for the construction of complex functional systems. [2][3][4][5][6] Because of the intrinsic large conformational flexibility of short-length peptides, amphiphilic, [7,8] or cyclic [9] scaffolds have been typically employed to ensure the formation of welldefined self-assembled structures. [2][3][4][5][6] Because of the intrinsic large conformational flexibility of short-length peptides, amphiphilic, [7,8] or cyclic [9] scaffolds have been typically employed to ensure the formation of welldefined self-assembled structures.

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mentioning

confidence: 99%

Unprecedented Molecular Architectures by the Controlled Self‐Assembly of a β‐Peptide Foldamer

et al. 2010

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Nature utilizes the self-assembly of monomeric units by multiple noncovalent interactions for the construction of complex functional systems.[1] In recent decades, a variety of peptide-based scaffolds, which range from simple aromatic dipeptides to small protein fragments, have been studied in order to understand the underlying mechanism and mimic this process to create artificial nano-and microstructures. [2][3][4][5][6] Because of the intrinsic large conformational flexibility of short-length peptides, amphiphilic, [7,8] or cyclic [9] scaffolds have been typically employed to ensure the formation of welldefined self-assembled structures. However, in contrast to the morphologies found in inorganic nanostructures, [10] the morphologies of the peptide-based self-assembled nano-and microstructures are limited to round shapes such as spheres, tubes, and rods.[11] The ability to construct biocompatible peptide-based molecular architectures with anisotropic shapes should expand the possibilities for the design of molecular machines for diverse applications in biological and materials science.[12] Such a construction should be possible if a molecular design principle for monomeric units held together by comparable intermolecular interactions in three orthogonal directions was available; however, currently this is not the case. [13] On the other hand, b peptides (oligomers of b amino acids) are excellent artificial peptides that can mimic proteinlike secondary structures such as helices, strands, and turns. [14] The self-associating behavior of b peptides have recently been investigated, [15][16][17][18] but the construction of higher-order structures with specific morphologies is still in its infancy. Herein we report the first example of highly homogeneous, welldefined, and finite molecular architectures formed by the selfassembly of a helical b peptide in aqueous solution. The 3D shapes of the assembled nano-and microstructures can be controlled by simply changing the experimental conditions.We used a homo-oligomer of trans-(S,S)-2-aminocyclopentanecarboxylic acid (ACPC) as a building block for the self-assembly. This particular b peptide resembles an a-helical peptide in terms of handedness, helical pitch, and the direction of the macrodipole moment, but is known to adopt a more stable and unique helical conformation through intramolecular 12-membered hydrogen bonding between C=O (i) and NÀH (i + 3) (the so-called 12-helix) in both solid state and solution, if the number of monomers exceeds approximately six residues (Figure 1 a). [19] Figure 1 b shows the chemical structure of the ACPC heptamer (ACPC 7 ), which is a highly hydrophobic molecule (aspect ratio % 2), because the methylene units of the cyclopentane rings are displayed over the helical faces, and both the N-and Ctermini are protected by a tert-butyloxycarbonyl (Boc) and a benzyl group, respectively. The possible modes of selfassembly of ACPC oligomers are illustrated in Figure 1 c. With this simple design, ACPC 7 should adopt a stable righthanded 12-heli...

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“…The self-assembly mechanism depends on the preparation conditions such as solvent polarity, pH, concentration, and temperature. [3][4][5] The L , L -diphenylalanine micro/nanostructures (FF-MNS) have a good thermal and chemical stability. [ 1 ] The solid-vapor phase synthesis results in a dense network of horizontal FF-MNS on different substrates.…”

Section: Doi: 101002/admi201500265mentioning

confidence: 99%

Self‐Assembled Peptide–Polyfluorene Nanocomposites for Biodegradable Organic Electronics

Khanra

Cipriano

Lam

et al. 2015

Adv Materials Inter

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Based on self‐assembly and mimicking strategies occurring in nature, peptide nanomaterials play a unique role in a new generation of hybrid materials for the electronics of the 21st century. This report describes the functionalization of diphenylalanine (FF)‐based micro/nanostructures with blue‐emitting conducting polymers of the polyfluorene (PF) family. The FF:PF polymer nanocomposites are synthesized by a liquid‐vapor phase method. Electron microscopy images reveal di‐octyl‐substituted PF (PF8) to bind better to the FF micro/nanotubes in comparison with ethyl‐hexyl PF (PF2/6), which influences its optical properties. Molecular dynamics simulations of FF nanotubes with monomeric units of PFs show that PF8 favors greater proximity to the grooves on the surface of the nanotubes due to a higher van der Waals interaction energy compared to PF2/6. The FF:PF nanocomposites are further utilized in light‐emitting diodes. Biodegradability tests from FF:PF8 nanocomposite films show more than 80% weight loss in 2 h by enzymatic action compared to PF8 pristine films, which do not degrade. Self‐assembly of FF nanostructures with organic semiconductors opens up a new generation of biocompatible and biodegradable materials in organic electronics.

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Bionanosphere Lithography via Hierarchical Peptide Self‐Assembly of Aromatic Triphenylalanine

Cited by 63 publications

References 45 publications

Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites

Hierarchical self-assembly of di-, tri- and tetraphenylalanine peptides capped with two fluorenyl functionalities: from polymorphs to dendrites

Unprecedented Molecular Architectures by the Controlled Self‐Assembly of a β‐Peptide Foldamer

Self‐Assembled Peptide–Polyfluorene Nanocomposites for Biodegradable Organic Electronics

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