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• W2091215316 startingPage "3502" @default.
• W2091215316 abstract "Three terminally protected short peptides Bis[Boc–D-Leu(1)–Cys(2)–OMe] 1, Bis[Boc–Leu(1)–Cys(2)–OMe] 2 and Bis[Boc–Val(1)–Cys(2)–OMe] 3 exhibit amyloid-like fibrillar morphology. Single crystal X-ray diffraction analysis of peptide 1 clearly demonstrates that it adopts an overall extended backbone molecular conformation that self-assembles to form an intermolecular hydrogen-bonded antiparallel supramolecular β-sheet structure in crystals. Scanning electron microscopic (SEM) images, transmission electron microscopic (TEM) images and Congo red binding studies vividly demonstrate the amyloid-like fibril formation of peptides 1, 2 and 3. However, after reduction of the disulfide bridge of peptides 1, 2 and 3, three newly generated peptides Boc–D-Leu(1)–Cys(2)–OMe 4, Boc–Leu(1)–Cys(2)–OMe 5 and Boc–Val(1)–Cys(2)–OMe 6 are formed and all of them failed to form any kind of fibril under the same conditions, indicating the important role of the disulfide bond in amyloid-like fibrillogenesis in a peptide model system." @default.
• W2091215316 created "2016-06-24" @default.
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• W2091215316 date "2005-01-01" @default.
• W2091215316 modified "2023-10-16" @default.
• W2091215316 title "The role of the disulfide bond in amyloid-like fibrillogenesis in a model peptide system" @default.
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• W2091215316 doi "https://doi.org/10.1039/b509083k" @default.
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