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

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

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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.

Item Type:
Journal Article
Journal or Publication Title:
Angewandte Chemie International Edition
Additional Information:
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1600/1600
Subjects:
?? amyloid beta-peptidesbinding sitescarbon isotopesheparinhumansnuclear magnetic resonance, biomolecularpeptide fragmentsprotein bindingprotein structure, tertiarygeneral chemistrycatalysischemistry(all) ??
ID Code:
66257
Deposited By:
Deposited On:
17 Sep 2013 08:03
Refereed?:
Yes
Published?:
Published
Last Modified:
16 Jul 2024 09:26