https://www.selleckchem.com/pr....oducts/sb-415286.htm
In the presence of GAGs, on the other hand, the interaction of K16 with the GAGs increases the importance of the hydrophobic interactions during Aβ16-22 aggregation, which in turn yields parallel alignments. A templating and ordering effect of the GAGs on the Aβ16-22 aggregates is observed. In summary, this study provides new insight at the atomic level on GAG-amyloid interactions, strengthening the view that sulfation of the GAGs plays a major role in this context.Crystal structures of ligand-bound G-protein-coupled receptors provide
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