Stoichiometry-controlled secondary structure transition of amyloid-derived supramolecular dipeptide co-assemblies

Wei Ji, Chengqian Yuan, Priyadarshi Chakraborty, Sharon Gilead, Xuehai Yan, Ehud Gazit*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Conformational transitions of secondary structures are a crucial factor in many protein misfolding diseases. However, the actual transition of folded proteins into β-sheet-rich structures is not fully understood. Inhibition of aggregate formation, mediated by the β-sheet conformation, and control of the secondary structural transition of proteins and peptides could potentially attenuate the development of amyloid-associated diseases. Here we describe a stoichiometry-controlled secondary structure transition of amyloid-derived dipeptide assemblies from a β-sheet to supramolecular helix conformation through co-assembly with a bipyridine derivative. The transition is mainly mediated by the intermolecular hydrogen bonds and π-π interactions between the two components, which induce the altered stacking and conformation of the co-assemblies, as confirmed by experimental results and computational simulations. This work not only exemplifies a feasible strategy to disrupt the β-sheet conformation, underlying amyloid-like fibril formation, but also provides a conceptual basis for the future utilization of the helical nanostructures in various biological applications.

Original languageEnglish
Article number65
JournalCommunications Chemistry
Issue number1
StatePublished - 1 Dec 2019


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