Using the bending beam model to estimate the elasticity of diphenylalanine nanotubes
The core recognition motif of the amyloidogenic beta-amyloid polypeptide, diphenylalanine peptide, has previously been shown to self-assemble into discrete, well-ordered, stiff nanotubes under mild conditions. The nanotubes keep the same morphology from room temperature up to 100 degrees C. In the p...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 23(2007), 14 vom: 03. Juli, Seite 7443-6 |
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| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2007
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Dipeptides phenylalanylphenylalanine 2577-40-4 Phenylalanine 47E5O17Y3R |
| Zusammenfassung: | The core recognition motif of the amyloidogenic beta-amyloid polypeptide, diphenylalanine peptide, has previously been shown to self-assemble into discrete, well-ordered, stiff nanotubes under mild conditions. The nanotubes keep the same morphology from room temperature up to 100 degrees C. In the presented study, we applied the bending beam model to atomic force microscopy images of diphenylalanine nanotubes suspended across cavities and obtained the Young's modulus 27 +/- 4 GPa and the shear modulus 0.21 +/- 0.03 GPa. We also showed that the elasticity of these nanotubes is stable within the same temperature range and at relative humidity from 0% to 70%. This study furthers our understanding of the structure and properties of these nanotubes, which are important for their potential applications in biotechnology |
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| Beschreibung: | Date Completed 14.09.2007 Date Revised 03.12.2021 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |