Terminal is important for the helicity of the self-assemblies of dipeptides derived from alanine
The organization of peptides and proteins attracts much attention, due to the biofunctionalities of the self-assemblies. Herein, four dipeptides derived from alanine were synthesized. It was found that the handedness of their self-assemblies was controlled by the chirality of the alanines at the ter...
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 29(2013), 20 vom: 21. Mai, Seite 6013-7 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2013
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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 Alanine OF5P57N2ZX |
| Zusammenfassung: | The organization of peptides and proteins attracts much attention, due to the biofunctionalities of the self-assemblies. Herein, four dipeptides derived from alanine were synthesized. It was found that the handedness of their self-assemblies was controlled by the chirality of the alanines at the terminals. The organic self-assemblies were studied using circular dichroism, (1)H NMR, Fourier transform infrared, field-emission electron microscopy, transmission electron microscopy, and X-ray diffraction. The results indicated that the electrostatic interactions among the carboxylate groups and H-bondings among the amide groups at the terminals play important roles in the formation of the organic self-assemblies |
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| Beschreibung: | Date Completed 11.12.2013 Date Revised 21.05.2013 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1520-5827 |
| DOI: | 10.1021/la400910g |