Related Experiment Video
Updated: May 16, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy
Jillian Madine1, Maya J Pandya, Matthew R Hicks
1Institute of Integrative Biology, University of Liverpool, UK.
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.

