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Supramolecular parallel beta-sheet and amyloid-like fibril forming peptides using delta-aminovaleric acid residue

Banerjee, A., Das, A.K. and Drew, M.G.B. (2005) Supramolecular parallel beta-sheet and amyloid-like fibril forming peptides using delta-aminovaleric acid residue. Tetrahedron, 61 (24). pp. 5906-5914. ISSN 0040-4020

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To link to this item DOI: 10.1016/j.tet.2005.03.100

Abstract/Summary

Four terminally blocked tripeptides containing delta-aminovaleric acid residue self-assemble to form supramolecular beta-sheet structures as are revealed from their FT-IR data. Single crystal X-ray diffraction studies of two representative peptides also show that they form parallel beta-sheet structures. Self-aggregation of these beta-sheet forming peptides leads to the formation of fibrillar structures, as is evident from scanning electron microscopic (SEM) and transmission electron microscopic (TEM) images. These peptide fibrils bind to a physiological dye, Congo red and exhibit a typical green-gold birefringence under polarized light, showing close resemblance to neurodegenerative disease causing amyloid fibrils. (c) 2005 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:10984
Uncontrolled Keywords:delta-aminovaleric acid, supramolecular parallel beta-sheet, amyloid-like fibril, OMEGA-AMINO ACIDS, ALZHEIMERS-DISEASE, PROTEIN FIBRILLOGENESIS, PARKINSONS-DISEASE, ALPHA-SYNUCLEIN, PLEATED-SHEET, PRION PROTEIN, LEWY, BODIES, SOLID-STATE, OLIGOPEPTIDES

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