Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy
AU - Madine, Jillian
AU - Pandya, Maya J
AU - Hicks, Matthew R
AU - Rodger, Alison
AU - Yates, Edwin A
AU - Radford, Sheena E
AU - Middleton, David A
N1 - Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
PY - 2012/12/21
Y1 - 2012/12/21
N2 - 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.
AB - 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.
KW - Amyloid beta-Peptides
KW - Binding Sites
KW - Carbon Isotopes
KW - Heparin
KW - Humans
KW - Nuclear Magnetic Resonance, Biomolecular
KW - Peptide Fragments
KW - Protein Binding
KW - Protein Structure, Tertiary
UR - http://www.scopus.com/inward/record.url?scp=84871953993&partnerID=8YFLogxK
U2 - 10.1002/anie.201204459
DO - 10.1002/anie.201204459
M3 - Journal article
C2 - 23161730
VL - 51
SP - 13140
EP - 13143
JO - Angewandte Chemie International Edition
JF - Angewandte Chemie International Edition
SN - 1433-7851
IS - 52
ER -