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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 Aβ 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 β-amyloid peptide, adopted β-sheet...
Four terminally blocked tripeptides containing δ-aminovaleric acid residue self-assemble to form supramolecular β-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 β-sheet structures. Self-aggregation of these β-sheet forming peptides leads to the formation of fibrillar structures, as is...
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