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

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 pol...

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Autores principales:	Mohammed A. Abosheasha, Toru Itagaki, Yoshihiro Ito, Motoki Ueda
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	helix–helix interaction helix orientation secondary structure peptide assembly Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/8d3ff4f8d2654efebd8a35cfcd281e74
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spelling	oai:doaj.org-article:8d3ff4f8d2654efebd8a35cfcd281e742021-11-11T17:27:46ZTubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides10.3390/ijms2221120751422-00671661-6596https://doaj.org/article/8d3ff4f8d2654efebd8a35cfcd281e742021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/12075https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The 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 (<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>6</sub> 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 (<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>2</sub>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib)<sub>2</sub>-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>2</sub> 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-<i>b</i>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib)-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>6</sub>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib) (SA2L12A2) and PSar-b-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>8</sub> (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.Mohammed A. AbosheashaToru ItagakiYoshihiro ItoMotoki UedaMDPI AGarticlehelix–helix interactionhelix orientationsecondary structurepeptide assemblyBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12075, p 12075 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	helix–helix interaction helix orientation secondary structure peptide assembly Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	helix–helix interaction helix orientation secondary structure peptide assembly Biology (General) QH301-705.5 Chemistry QD1-999 Mohammed A. Abosheasha Toru Itagaki Yoshihiro Ito Motoki Ueda Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
description	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 (<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>6</sub> 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 (<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>2</sub>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib)<sub>2</sub>-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>2</sub> 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-<i>b</i>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib)-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>6</sub>-(<span style="font-variant: small-caps;">l</span>-Ala-Aib) (SA2L12A2) and PSar-b-(<span style="font-variant: small-caps;">l</span>-Leu-Aib)<sub>8</sub> (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.
format	article
author	Mohammed A. Abosheasha Toru Itagaki Yoshihiro Ito Motoki Ueda
author_facet	Mohammed A. Abosheasha Toru Itagaki Yoshihiro Ito Motoki Ueda
author_sort	Mohammed A. Abosheasha
title	Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
title_short	Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
title_full	Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
title_fullStr	Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
title_full_unstemmed	Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides
title_sort	tubular assembly formation induced by leucine alignment along the hydrophobic helix of amphiphilic polypeptides
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/8d3ff4f8d2654efebd8a35cfcd281e74
work_keys_str_mv	AT mohammedaabosheasha tubularassemblyformationinducedbyleucinealignmentalongthehydrophobichelixofamphiphilicpolypeptides AT toruitagaki tubularassemblyformationinducedbyleucinealignmentalongthehydrophobichelixofamphiphilicpolypeptides AT yoshihiroito tubularassemblyformationinducedbyleucinealignmentalongthehydrophobichelixofamphiphilicpolypeptides AT motokiueda tubularassemblyformationinducedbyleucinealignmentalongthehydrophobichelixofamphiphilicpolypeptides
_version_	1718432075769446400

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

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