Madine, Jillian and Pandya, Maya J and Hicks, Matthew R and Rodger, Alison and Yates, Edwin A and Radford, Sheena E and Middleton, David A (2012) Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy. Angewandte Chemie International Edition, 51 (52). pp. 13140-3. ISSN 1433-7851
Full text not available from this repository.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.