Chirality-Driven Parallel and Antiparallel β-Sheet Secondary Structures of Phe-Ala Lipodipeptides
Four Phe-Ala lipodipeptides with different stereochemical structures are observed to self-assemble into twisted nanoribbons in water. The handedness of the twisted nanoribbons is controlled by the chirality of the phenylalanine near the alkyl chain, while the stacking handedness of the phenyl and ca...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 33(2017), 33 vom: 22. Aug., Seite 8246-8252 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2017
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Dipeptides Lipids Phenylalanine 47E5O17Y3R Alanine OF5P57N2ZX |
| Zusammenfassung: | Four Phe-Ala lipodipeptides with different stereochemical structures are observed to self-assemble into twisted nanoribbons in water. The handedness of the twisted nanoribbons is controlled by the chirality of the phenylalanine near the alkyl chain, while the stacking handedness of the phenyl and carbonyl groups is determined by the alanine at the C-terminal. The homochiral and heterochiral lipodipeptides self-assemble into parallel and antiparallel β-sheet structures, respectively. The 1H NMR, FTIR, X-ray diffraction, and circular dichroism characterizations indicate that these phenomena are mainly driven by the interaction between neighboring phenyl groups and H-bonding among the amide groups |
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| Beschreibung: | Date Completed 16.01.2019 Date Revised 16.01.2019 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/acs.langmuir.7b01942 |