Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes
Self-assembled peptide nanofibers (NFs) obtained from β-sheet peptides conjugated with drugs, including antigenic peptides, have recently attracted significant attention. However, extensive studies on the interactions of β-sheet peptide NFs with model cell membranes have not been reported. In this s...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/24/9518 |
| _version_ | 1797544677323309056 |
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| author | Tomonori Waku Ayane Kasai Akio Kobori Naoki Tanaka |
| author_facet | Tomonori Waku Ayane Kasai Akio Kobori Naoki Tanaka |
| author_sort | Tomonori Waku |
| collection | DOAJ |
| description | Self-assembled peptide nanofibers (NFs) obtained from β-sheet peptides conjugated with drugs, including antigenic peptides, have recently attracted significant attention. However, extensive studies on the interactions of β-sheet peptide NFs with model cell membranes have not been reported. In this study, we investigated the interactions between three types of NFs, composed of PEG-peptide conjugates with different ethylene glycol (EG) lengths (6-, 12- and 24-mer), and dipalmitoylphosphatidylcholine (DPPC) Langmuir membranes. When increasing the EG chain length, those interactions significantly decreased considering measurements in the presence of the NFs of: (i) changes in surface pressure of the DPPC Langmuir monolayers and (ii) surface pressure–area (π–<i>A</i>) compression isotherms of DPPC. Because the observed trend was similar to the EG length dependency with regard to cellular association and cytotoxicity of the NFs that was reported previously, the interaction of NFs with phospholipid membranes represented a crucial factor to determine the cellular association and toxicity of the NFs. In contrast to NFs, no changes were observed with varying EG chain length on the interaction of the building block peptide with the DPPC membrane. The results obtained herein can provide a design guideline on the formulation of β-sheet peptide NFs, which may broaden its potential. |
| first_indexed | 2024-03-10T14:04:55Z |
| format | Article |
| id | doaj.art-727c70ca7b4f427281c0715c55a8c012 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T14:04:55Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-727c70ca7b4f427281c0715c55a8c0122023-11-21T00:48:37ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-12-012124951810.3390/ijms21249518Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell MembranesTomonori Waku0Ayane Kasai1Akio Kobori2Naoki Tanaka3Faculty of Molecular Chemistry and Engineering, Kyoto Institute of Technology, Gosyokaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, JapanFaculty of Molecular Chemistry and Engineering, Kyoto Institute of Technology, Gosyokaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, JapanFaculty of Molecular Chemistry and Engineering, Kyoto Institute of Technology, Gosyokaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, JapanFaculty of Molecular Chemistry and Engineering, Kyoto Institute of Technology, Gosyokaido-cho, Matsugasaki, Sakyo-ku, Kyoto 606-8585, JapanSelf-assembled peptide nanofibers (NFs) obtained from β-sheet peptides conjugated with drugs, including antigenic peptides, have recently attracted significant attention. However, extensive studies on the interactions of β-sheet peptide NFs with model cell membranes have not been reported. In this study, we investigated the interactions between three types of NFs, composed of PEG-peptide conjugates with different ethylene glycol (EG) lengths (6-, 12- and 24-mer), and dipalmitoylphosphatidylcholine (DPPC) Langmuir membranes. When increasing the EG chain length, those interactions significantly decreased considering measurements in the presence of the NFs of: (i) changes in surface pressure of the DPPC Langmuir monolayers and (ii) surface pressure–area (π–<i>A</i>) compression isotherms of DPPC. Because the observed trend was similar to the EG length dependency with regard to cellular association and cytotoxicity of the NFs that was reported previously, the interaction of NFs with phospholipid membranes represented a crucial factor to determine the cellular association and toxicity of the NFs. In contrast to NFs, no changes were observed with varying EG chain length on the interaction of the building block peptide with the DPPC membrane. The results obtained herein can provide a design guideline on the formulation of β-sheet peptide NFs, which may broaden its potential.https://www.mdpi.com/1422-0067/21/24/9518nanofiberDPPC Langmuir membraneπ–<i>A</i> isothermdrug delivery system |
| spellingShingle | Tomonori Waku Ayane Kasai Akio Kobori Naoki Tanaka Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes International Journal of Molecular Sciences nanofiber DPPC Langmuir membrane π–<i>A</i> isotherm drug delivery system |
| title | Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes |
| title_full | Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes |
| title_fullStr | Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes |
| title_full_unstemmed | Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes |
| title_short | Investigation on the Interactions between Self-Assembled β-Sheet Peptide Nanofibers and Model Cell Membranes |
| title_sort | investigation on the interactions between self assembled β sheet peptide nanofibers and model cell membranes |
| topic | nanofiber DPPC Langmuir membrane π–<i>A</i> isotherm drug delivery system |
| url | https://www.mdpi.com/1422-0067/21/24/9518 |
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