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Hydrogen-bonded dimer can mediate supramolecular beta-sheet formation and subsequent amyloid-like fibril formation: a model study

Banerjee, A. , Maji, S.K., Drew, M.G.B., Haldar, D., Das, A.K. and Banerjee, A. (2004) Hydrogen-bonded dimer can mediate supramolecular beta-sheet formation and subsequent amyloid-like fibril formation: a model study. Tetrahedron, 60 (28). pp. 5935-5944. ISSN 0040-4020

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To link to this item DOI: 10.1016/j.tet.2004.05.041

Abstract/Summary

FT-IR data of six terminally blocked tripeptides containing Acp (epsilon-aminocaproic acid) reveals that all of them form supramolecular beta-sheets in the solid state. Single crystal X-ray diffraction studies of two peptides not only support this data but also disclose the fact that the supramolecular beta-sheet formation is initiated via dimer formation. The Scanning Electron Microscopic images of all peptides exhibit amyloid-like fibrils that show green birefringence after binding with Congo red, which is a characteristic feature of many neurodegenerative disease causing amyloid fibrils. (C) 2004 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:10988
Uncontrolled Keywords:self-assembling peptides, dimer, Aib, beta-sheet, amyloid-like fibrils , X-RAY-DIFFRACTION, SOLID-STATE NMR, PAIRED HELICAL FILAMENTS, ATOMIC-FORCE MICROSCOPY, ALZHEIMERS-DISEASE, CRYSTALLOGRAPHIC SIGNATURE, PROTEIN FIBRILLOGENESIS, MOLECULAR DUPLEXES, FOLDING PROBLEM, PLEATED-SHEET

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