title: beta-Sheet mediated self-assembly of dipeptides of omega-amino acids and remarkable fibrillation in the solid state.
abstract: Single crystal X-ray diffraction studies show that the extended structure of dipeptide 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 beta-sheet structure. In dipeptide 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 and 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.
authors: Department of Chemistry, University of Calcutta, 92, A. P. C. Road, Kolkata 700009, India.
authors: Anita
authors: A
authors: Dutt
authors: Michael G B
authors: MG
authors: Drew
authors: Animesh
authors: A
authors: Pramanik
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D004151:Dipeptides / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular; D013055:Spectrophotometry, Infrared
chemical_list: D000596:Amino Acids; D004151:Dipeptides