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

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Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy. / Madine, Jillian; Pandya, Maya J; Hicks, Matthew R et al.

In: Angewandte Chemie International Edition, Vol. 51, No. 52, 21.12.2012, p. 13140-3.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Madine, J, Pandya, MJ, Hicks, MR, Rodger, A, Yates, EA, Radford, SE & Middleton, DA 2012, 'Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy', Angewandte Chemie International Edition, vol. 51, no. 52, pp. 13140-3. https://doi.org/10.1002/anie.201204459

APA

Madine, J., Pandya, M. J., Hicks, M. R., Rodger, A., Yates, E. A., Radford, S. E., & Middleton, D. A. (2012). Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy. Angewandte Chemie International Edition, 51(52), 13140-3. https://doi.org/10.1002/anie.201204459

Vancouver

Madine J, Pandya MJ, Hicks MR, Rodger A, Yates EA, Radford SE et al. Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy. Angewandte Chemie International Edition. 2012 Dec 21;51(52):13140-3. doi: 10.1002/anie.201204459

Author

Madine, Jillian ; Pandya, Maya J ; Hicks, Matthew R et al. / Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy. In: Angewandte Chemie International Edition. 2012 ; Vol. 51, No. 52. pp. 13140-3.

Bibtex

@article{f1e08293823147998358da59675da798,
title = "Site-specific identification of an aβ fibril-heparin interaction site by using solid-state NMR spectroscopy",
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.",
keywords = "Amyloid beta-Peptides, Binding Sites, Carbon Isotopes, Heparin, Humans, Nuclear Magnetic Resonance, Biomolecular, Peptide Fragments, Protein Binding, Protein Structure, Tertiary",
author = "Jillian Madine and Pandya, {Maya J} and Hicks, {Matthew R} and Alison Rodger and Yates, {Edwin A} and Radford, {Sheena E} and Middleton, {David A}",
note = "Copyright {\textcopyright} 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",
year = "2012",
month = dec,
day = "21",
doi = "10.1002/anie.201204459",
language = "English",
volume = "51",
pages = "13140--3",
journal = "Angewandte Chemie International Edition",
issn = "1433-7851",
publisher = "Wiley-VCH Verlag",
number = "52",

}

RIS

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 -