. Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution. PLoS One. 2011;6(7):e21776. PubMed.


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  1. Pande's group introduces a D-proline at position 37 of the Aβ sequence, which is incompatible with the fibril cross-β structure. This will certainly keep their peptide away from the fibril state, stopping aggregation at the oligomer level. In these oligomers, they see a turn at fragment 24-27, which has been observed by us and a number of other groups. This new peptide could potentially be an addition to the growing arsenal of oligomer-forming model peptides, but, unfortunately, there are really no experiments to validate it in a biological context. They provide no data on reactivity with conformational antibodies or cell assays to measure toxicity, for example. Still, this work is confirmatory, and at a protein engineering level, introducing clever non-natural amino acid substitutions is a cool thing to do. Moreover, the quality of the NMR data is good and might perhaps in further work yield more information about the 3D-structure of these oligomers, which would give all of us something new to test or build on.

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