Ontology highlight
ABSTRACT:
SUBMITTER: Madine J
PROVIDER: S-EPMC3749465 | biostudies-literature | 2012 Dec
REPOSITORIES: biostudies-literature
Madine Jillian J Pandya Maya J MJ Hicks Matthew R MR Rodger Alison A Yates Edwin A EA Radford Sheena E SE Middleton David A DA
Angewandte Chemie (International ed. in English) 20121114 52
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. ...[more]