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 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.