Haldar, Debasish ; Drew, Michael G. B. ; Banerjee, Arindam (2006) α-Aminoisobutyric acid modified protected analogues of β-amyloid residue 17–20: a change from sheet to helix Tetrahedron, 62 (26). pp. 6370-6378. ISSN 0040-4020
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Official URL: http://www.sciencedirect.com/science/article/pii/S...
Related URL: http://dx.doi.org/10.1016/j.tet.2006.04.036
Abstract
The strong intermolecular interactions mediated by short hydrophobic sequences (e.g., 17-20, -L-Leu-L-Val-L-Phe-L-Phe-) in the middle of A beta are known to play a crucial role in the neuropathology of Alzheimer's disease. FTIR, TEM and Congo red binding studies indicated that a series of L-Ala substituted terminally protected peptides related to the sequence 17-20 of the beta-amyloid peptide, adopted D-sheet conformations. However, the Aib-modified analogues disrupt the D-sheet structure and switch over to a 310 helix with increasing number of Aib residues. X-ray crystallography shed some light on the change from sheet to helix at atomic resolution.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | Amyloid Beta-Peptide; Amyloid-Like Fibril; Aib; Supramolecular; Beta-Sheet; Beta-Turn; 3(10) Helix; Solid-State Nmr; 1st Crystallographic Signature; Fibril Formation; Alzheimers-Disease; Protein Fibrillogenesis; Amino-Acid; Peptide; Fragments; Model; Conformations |
| ID Code: | 99548 |
| Deposited On: | 04 Nov 2016 12:25 |
| Last Modified: | 04 Nov 2016 12:25 |
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