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Self-assembling tripeptide as organogelator: the role of aromatic π-stacking interactions in gel formation.
- Source :
-
Supramolecular Chemistry . Feb2010, Vol. 22 Issue 2, p95-102. 8p. 2 Color Photographs, 3 Black and White Photographs, 2 Diagrams, 3 Charts, 6 Graphs. - Publication Year :
- 2010
-
Abstract
- While the terminally protected tripeptide Boc-Phe-Gly-m-ABA-OMe I (m-ABA, meta-amino benzoic acid) is an excellent gelator of aromatic organic solvents, another similar tripeptide Boc-Leu-Gly-m-ABA-OMe II, where the Phe residue of peptide I is replaced by Leu, cannot form gels with the same solvents. The morphology of the gels of peptide I, characterised by the field-emission scanning electron microscopy and high-resolution transmission electron microscopy, reveals the formation of nanofibrous networks which are known to encapsulate solvent molecules to form gels. The wide-angle X-ray scattering studies of the gels suggest the β-sheet-mediated self-assembly of peptide I in the formation of a nanofibrous network, where π-stacking interactions of Phe play an important role in the self-assembly and gel formation. The dried gel of peptide I observed between crossed polarisers after binding with a physiological dye, Congo red, shows a bluish-green birefringence, a characteristic of amyloid fibrils. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10610278
- Volume :
- 22
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Supramolecular Chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 49145274
- Full Text :
- https://doi.org/10.1080/10610270903254142