title: Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy.
abstract: At the surface of Aβ(1-40) amyloid fibrils that have a threefold molecular symmetry (green in the left picture) a site of interaction of the glycosaminoglycan analogue heparin (blue) was identified. The binding site consists of residues at the N terminus and the turn regions defining the apices of the triangular geometry. Heparin has a lower affinity for Aβ(1-40) fibrils having twofold molecular symmetry, thus revealing a remarkable morphological selectivity.
authors.affiliation: Institute of Integrative Biology, University of Liverpool, UK.
authors.forename: Jillian
authors.initials: J
authors.lastname: Madine
authors.forename: Maya J
authors.initials: MJ
authors.lastname: Pandya
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Hicks
authors.forename: Alison
authors.initials: A
authors.lastname: Rodger
authors.forename: Edwin A
authors.initials: EA
authors.lastname: Yates
authors.forename: Sheena E
authors.initials: SE
authors.lastname: Radford
authors.forename: David A
authors.initials: DA
authors.lastname: Middleton
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D002247:Carbon Isotopes / Q000737:chemistry; D006493:Heparin / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D016229:Amyloid beta-Peptides; D002247:Carbon Isotopes; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D006493:Heparin