A New Artificial β-Sheet That Dimerizes through Parallel β-Sheet Interactions
journal contributionposted on 19.02.2009 by Sergiy Levin, James S. Nowick
Any type of content formally published in an academic journal, usually following a peer-review process.
This paper introduces a chemical model of a β-sheet that dimerizes through parallel β-sheet interactions in CDCl3 solution. The model consists of two C-terminally linked dipeptides connected to a molecular template. 1H NMR studies establish the β-sheet folding and dimerization of the model system. This system corroborates that linking two peptide strands and blocking one edge of the assembly creates soluble, easy-to-study systems that participate in the types of interactions that occur widely in peptide and protein aggregates.