beta-Sheet mediated self-assembly of dipeptides of omega-amino acids and remarkable fibrillation in the solid stateDutt, A., Drew, M.G.B. and Pramanik, A. (2005) beta-Sheet mediated self-assembly of dipeptides of omega-amino acids and remarkable fibrillation in the solid state. Organic & Biomolecular Chemistry, 3 (12). pp. 2250-2254. ISSN 1477-0520 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: 10.1039/b504112k Abstract/SummarySingle crystal X-ray diffraction studies show that the extended structure of dipeptide I Boc-beta-Ala-m-ABA-OMe (m-ABA: meta-aminobenzoic acid) self-assembles in the solid state by intermolecular hydrogen bonding to create an infinite parallel P-sheet structure. In dipeptide II Boc-gamma-Abu-m-ABA-OMe (gamma-Abu: gamma-aminobutyric acid), two such parallel beta-sheets are further cross-linked by intermolecular hydrogen bonding through m-aminobenzoic acid moieties. SEM (scanning electron microscopy) studies reveal that both the peptides I and II form amyloid-like fibrils in the solid state. The fibrils are also found to be stained readily by Congo red, a characteristic feature of the amyloid fiber whose accumulation causes several fatal diseases such as Alzheimer's, prion-protein etc.
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