NMR characterization of the interaction of GroEL with amyloid β as a model ligand
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Updated: May 12, 2026

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
Maho Yagi-Utsumi1, Tomoko Kunihara, Takashi Nakamura
1Institute for Molecular Science and Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Myodaiji, Okazaki, Japan.
Abstract:
Here we report an NMR study on the substrate interaction modes of GroEL using amyloid β (Aβ) as a model ligand. We found that GroEL could suppress Aβ(1-40) amyloid formation by interacting with its two hydrophobic segments Leu17-Ala21 and Ala30-Val36, which involve key residues in fibril formation. The binding site of Aβ(1-40) was mapped on a pair of α-helices located in the GroEL apical domain. These results provide insights into chaperonin recognition of amyloidogenic proteins of pathological interest.
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