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Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy

Research output: Contribution to Journal/MagazineJournal articlepeer-review

  • Jillian Madine
  • Maya J Pandya
  • Matthew R Hicks
  • Alison Rodger
  • Edwin A Yates
  • Sheena E Radford
  • David A Middleton
<mark>Journal publication date</mark>21/12/2012
<mark>Journal</mark>Angewandte Chemie International Edition
Issue number52
Number of pages4
Pages (from-to)13140-3
Publication StatusPublished
<mark>Original language</mark>English


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.

Bibliographic note

Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.