Haldar, Debasish ; Banerjee, Arindam (2007) Intrinsic amyloidogenic behavior of terminally protected Alzheimer's Aβ17-21 peptide: self-aggregation and amyloid-like fibril formation International Journal of Peptide Research and Therapeutics, 13 (3). pp. 439-446. ISSN 1573-3149
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Official URL: http://link.springer.com/article/10.1007%2Fs10989-...
Related URL: http://dx.doi.org/10.1007/s10989-006-9072-x
Abstract
The terminally protected peptide Boc-Leu-Val-Phe-Phe-Ala-OMe bearing sequence similarity with the central hydrophobic cluster (CHC) of Alzheimer’s Aβ17-21 peptide self-assembles to produce amyloid-like straight unbranched fibrils from organic solvents. The fibrils readily bind with a physiological dye Congo red (CR) and exhibits green gold birefringence under polarized light, a characteristic feature of amyloid plaque obtained from many neurodegenerative diseases. FTIR spectroscopy and in silico energy minimization study shed some light on the antiparallel supramolecular β-sheet aggregation of the peptide.
Item Type: | Article |
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Source: | Copyright of this article belongs to Springer. |
Keywords: | Alzheimer’s Aβ17-21 Peptide; Antiparallel Β-Sheet; Amyloid-Like Fibrils; Birefringence; CHC; Congo Red |
ID Code: | 99583 |
Deposited On: | 07 Nov 2016 10:44 |
Last Modified: | 07 Nov 2016 10:44 |
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