Integrated Nanostructures Based on Self-Assembled Amphiphilic Polypeptides

Ueda, Mitsuru; Müller, Stefan; Seo, Si‐Yoong; Rahman, Mofizur; Ito, Yoshihiro

doi:10.1021/bk-2017-1252.ch002

Cited by 7 publications

(15 citation statements)

References 19 publications

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“…The ethanol injection method initially formed curved sheets of SL12 in milli-Q water. After heat treatment at 90 °C for 1 h, the sheets spontaneously transformed into uniform tubular structures with a diameter of around 80 nm ( Figure 3 A,B,E), which corresponds to previous results [ 21 , 22 , 23 , 25 , 27 , 32 , 33 ]. In contrast, a spherical micelle and vesicle were observed in the dispersion of SL4A4L4, which had the same length of a 12 mer hydrophobic α-helical block as SL12 ( Figure 3 C,D).…”

Section: Resultssupporting

confidence: 90%

“…80 nm were prepared from an amphiphilic block copolypeptide, PSar n - b -( l -Leu-Aib) 6 (SL12) with a hydrophobic α-helix composed of the LxLxLxLxLxLx sequence, which involves two LxxxLxxxL sequences [ 20 , 21 ]. The phenomenon was explained by the hypothesis that the helical part is uniformly packed in a hydrophobic layer due to the concave–convex interaction between helices with the LxxxLxxxL sequence [ 20 , 21 , 22 , 23 ]. Kimura and coworkers demonstrated that PSar n - b -( l -Val-Aib) 6 did not form a nanotube [ 24 ], which showed the importance of the Leu side chain for morphology control.…”

Section: Introductionmentioning

confidence: 99%

“…Thus, although soft matter may spontaneously form from amphipathic molecules, its homogeneity and shape design are possible with the precise molecular orientation found in proteins. While it has been shown that SL12 assumes tube-forming packing, it has been reported that PSar n - b -( l -Leu-Aib) 8 (SL16) forms vesicle structures [ 23 , 25 , 26 ]. Hence, in this study, we investigated the importance of the LxxxLxxxL sequence of the hydrophobic helix for tubular assembly formation by comparing self-assembly prepared from four kinds of amphiphilic polypeptides, SL12, SL16, PSar- b -( l -Leu-Aib) 2 -( l -Ala-Aib) 2 -( l -Leu-Aib) 2 (SL4A4L4), and PSar- b -( l -Ala-Aib)-( l -Leu-Aib) 6 -( l -Ala-Aib) (SA2L12A2).…”

Section: Introductionmentioning

confidence: 99%

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Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides

Abosheasha

Itagaki

Ito

et al. 2021

IJMS

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The introduction of α-helical structure with a specific helix–helix interaction into an amphipathic molecule enables the determination of the molecular packing in the assembly and the morphological control of peptide assemblies. We previously reported that the amphiphilic polypeptide SL12 with a polysarcosine (PSar) hydrophilic chain and hydrophobic α-helix (l-Leu-Aib)6 involving the LxxxLxxxL sequence, which induces homo-dimerization due to the concave–convex interaction, formed a nanotube with a uniform 80 nm diameter. In this study, we investigated the importance of the LxxxLxxxL sequence for tube formation by comparing amphiphilic polypeptide SL4A4L4 with hydrophobic α-helix (l-Leu-Aib)2-(l-Ala-Aib)2-(l-Leu-Aib)2 and SL12. SL4A4L4 formed spherical vesicles and micelles. The effect of the LxxxLxxxL sequence elongation on tube formation was demonstrated by studying assemblies of PSar-b-(l-Ala-Aib)-(l-Leu-Aib)6-(l-Ala-Aib) (SA2L12A2) and PSar-b-(l-Leu-Aib)8 (SL16). SA2L12A2 formed nanotubes with a uniform 123 nm diameter, while SL16 assembled into vesicles. These results showed that LxxxLxxxL is a necessary and sufficient sequence for the self-assembly of nanotubes. Furthermore, we fabricated a double-layer nanotube by combining two kinds of nanotubes with 80 and 120 nm diameters—SL12 and SA2L12A2. When SA2L12A2 self-assembled in SL12 nanotube dispersion, SA2L12A2 initially formed a rolled sheet, the sheet then wrapped the SL12 nanotube, and a double-layer nanotube was obtained.

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Section: Resultssupporting

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides

Abosheasha

Itagaki

Ito

et al. 2021

IJMS

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“…We found a peptide-lipid hybrid vesicle (PLHV) composed of 1,2-dimyristoyl- sn -glycero-3-phosphocholine (DMPC) within a sea of amphiphilic block copolypeptides composed of poly(sarcosine) and poly( l -leucine-2-aminoisobutyric acid) (poly(Sar) 26 -( l -Leu-Aib) 7 , S26L14) (Figure ). The hydrophobic alternating Leu-Aib copolymer of S26L14 folds to form an α-helix structure that induces tight bundle packing between helices to facilitate formation of a polypeptide membrane, − and the spontaneous formation of a phase-separated membrane structure with a lipid was expected. As a result, the polypeptide domain controlled the uniform hybrid assembly and gating lipid domain, which allowed the temperature-responsive release of fluorescein isothiocyanate-labeled polyethylene glycol (FITC-PEG) due to its phase-transition phenomena.…”

Section: Introductionmentioning

confidence: 99%

Spontaneous Formation of Gating Lipid Domain in Uniform-Size Peptide Vesicles for Controlled Release

et al. 2018

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Hybrid assemblies composed of phospholipids and amphiphilic polymers have been investigated previously as a biomimetic model of biological cells. However, these studies focused on the functions of polymers in a sea of membrane lipids. Here, we prepared a highly stable peptide-lipid hybrid vesicle from a combination of an amphiphilic polypeptide and the phospholipid, 1,2-dimyristoyl-sn-glycero-3-phosphocholine, with a mixing molar ratio of 1:1. The phase-separated structure of the hybrid vesicle was demonstrated by fluorescence resonance energy transfer analysis. The lipid domain of the hybrid vesicle had a phasetransition temperature of 38 °C and allowed the permeation of a hydrophilic molecule, fluorescein isothiocyanate-labeled polyethylene glycol (M w : 2000), above 38 °C. The designed peptide-lipid hybrid vesicle and a "lipidic gate" are a promising tool for smart drug delivery.

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“…The preparation of phase-separated peptide assemblies using two different kinds of amphiphilic polypeptides has been reported, including a round-bottom flask shaped assembly, which was named the “assembly-patchwork system”. − The two kinds of amphiphilic polypeptides formed nanotubes of 200 nm in length and vesicle-forming nanosheets, respectively. Hydrophobic interactions between the edges of the nanosheet and the nanotube enabled the nanosheet to fuse and round up on the open ends of the nanotube, resulting in a round-bottom flask shaped assembly.…”

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confidence: 99%

End-Sealed High Aspect Ratio Hollow Nanotubes Encapsulating an Anticancer Drug: Torpedo-Shaped Peptidic Nanocapsules

et al. 2019

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Nanomaterial morphology is important for the targeted delivery of drugs to tissues as well as subsequent cellular uptake. Hollow nanotubes composed of peptides, with a diameter of 80 nm and various lengths (100, 200, 300, 600 nm), were successfully capped and sealed with a peptide hemisphere to encapsulate the anticancer drug, cisplatin. The torpedo-shaped nanocapsules with an aspect ratio (length/diameter) of 2.4 showed more rapid cellular uptake and accumulation at the tumor site compared with spherical analogues. Successful delivery of cisplatin to tumors was achieved in a mouse model and tumor growth was efficiently suppressed.

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Integrated Nanostructures Based on Self-Assembled Amphiphilic Polypeptides

Cited by 7 publications

References 19 publications

Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides

Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides

Spontaneous Formation of Gating Lipid Domain in Uniform-Size Peptide Vesicles for Controlled Release

End-Sealed High Aspect Ratio Hollow Nanotubes Encapsulating an Anticancer Drug: Torpedo-Shaped Peptidic Nanocapsules

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