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

ABSTRACT: At the surface of A?(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 A?(1-40) fibrils having twofold molecular symmetry, thus revealing a remarkable morphological selectivity.

SUBMITTER: Madine J

PROVIDER: S-EPMC3749465 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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

Madine Jillian J Pandya Maya J MJ Hicks Matthew R MR Rodger Alison A Yates Edwin A EA Radford Sheena E SE Middleton David A DA

Angewandte Chemie (International ed. in English) 20121114 52

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. ...[more]

PMID: 23161730

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