Accessibility navigation


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

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

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:Faculty of 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

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation