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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MDPI AG
2021-11-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/22/21/12075 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T05:59:53Z |
| format | Article |
| id | doaj.art-8d3ff4f8d2654efebd8a35cfcd281e74 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T05:59:53Z |
| publishDate | 2021-11-01 |
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| spelling | doaj.art-8d3ff4f8d2654efebd8a35cfcd281e742023-11-22T21:02:21ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-11-0122211207510.3390/ijms222112075Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic PolypeptidesMohammed A. Abosheasha0Toru Itagaki1Yoshihiro Ito2Motoki Ueda3RIKEN Cluster for Pioneering Research (CPR), Wako 351-0198, Saitama, JapanRIKEN Cluster for Pioneering Research (CPR), Wako 351-0198, Saitama, JapanRIKEN Cluster for Pioneering Research (CPR), Wako 351-0198, Saitama, JapanRIKEN Cluster for Pioneering Research (CPR), Wako 351-0198, Saitama, JapanThe 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.https://www.mdpi.com/1422-0067/22/21/12075helix–helix interactionhelix orientationsecondary structurepeptide assembly |
| spellingShingle | Mohammed A. Abosheasha Toru Itagaki Yoshihiro Ito Motoki Ueda Tubular Assembly Formation Induced by Leucine Alignment along the Hydrophobic Helix of Amphiphilic Polypeptides International Journal of Molecular Sciences helix–helix interaction helix orientation secondary structure peptide assembly |
| title | 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_short | 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 |
| topic | helix–helix interaction helix orientation secondary structure peptide assembly |
| url | https://www.mdpi.com/1422-0067/22/21/12075 |
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