Journal
SUPRAMOLECULAR CHEMISTRY
Volume 22, Issue 2, Pages 95-102Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/10610270903254142
Keywords
peptide; gelator; pi-stacking interactions; self-assembly; nanofibrous network
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Funding
- CSIR, New Delhi, India
- UGC, New Delhi [32190/2006(SR)]
- Nanoscience and Nanotechnology, University of Calcutta
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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 beta-sheet-mediated self-assembly of peptide I in the formation of a nanofibrous network, where pi-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.
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