Models of binding of 4′-nitrophenyl α-d-mannopyranoside to the lectin concanavalin A

Molecular models for the complex formed between the lectin concanavalin A (Con A) and the saccharide derivative 4′-nitrophenyl-α-d-mannopyranoside (α-PNM) are presented, combining evidence from 1H-n.m.r. measurements, semi-empirical energy calculations and interactive graphics modelling. The models are in good agreement with the experimental data. Close examination of the models suggests that hydrophobic interactions together with van der Waals interactions and hydrogen bonds contribute to the stability of the complexes. It appears that there is a limited number of possible modes of binding of α-PNM to Con A. © 1989

High-resolution NMR spectroscopy of the β-amyloid(1-28) fibril typical for Alzheimer's disease

Unlabeled samples of the β-amyloid peptide(1-28) fibrils typical of Alzheimer's disease could be used to obtain well-resolved one- and two-dimensional 1H NMR spectra (see picture). The technique applied was high-resolution magic-angle spinning on a 600 MHz NMR spectrometer. The results are in agreement with a parallel, in-register arrangement of the β-amyloid peptide in the fibril