Inhibitor-Mediated Structural Transition in a Minimal Amyloid Model

Priyadarshi Chakraborty, Santu Bera, Phil Mickel, Ashim Paul, Linda J.W. Shimon, Zohar A. Arnon, Daniel Segal, Petr Král, Ehud Gazit*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Despite the fundamental clinical importance of amyloid fibril formation, its mechanism is still enigmatic. Crystallography of minimal amyloid models was a milestone in the understanding of the architecture and biological activities of amyloid fibers. However, the crystal structure of ultimate dipeptide-based amyloids is not yet reported. Herein, we present the crystal structure of a typical amyloid-forming minimal dipeptide, Ac-Phe-Phe-NH2 (Ac-FF-NH2), showing a canonical β-sheet structure at the atomic level. The simplicity of the structure helped in investigating amyloid-inhibition using crystallography, never previously reported for larger peptide models. Interestingly, in the presence of an inhibitor, the supramolecular packing of Ac-FF-NH2 molecules rearranged into a supramolecular 2-fold helix (21 helix). This study promotes our understanding of the mechanism of amyloid formation and of the structural transitions that occur during the inhibition process in a most fundamental model.

Original languageEnglish
Article numbere202113845
JournalAngewandte Chemie - International Edition
Issue number3
StatePublished - 17 Jan 2022


FundersFunder number
Advanced ERC
Horizon 2020 Framework Programme694426
Horizon 2020 Framework Programme
European Research Council
Tel Aviv University
Horizon 2020


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