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Updated: May 22, 2026

Experimental Approaches for Biochemical Analysis of Glial Fibrillary Acidic Protein and Its Disease-associated Variants
Published on: November 28, 2025
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone
Jin Chen1, Hisashi Yagi, Pietro Sormanni
1Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, Myodaiji, Okazaki, Japan. jinchen@ims.ac.jp
Abstract:
The chaperonin GroEL plays an essential role in promoting protein folding and in protecting against misfolding and aggregation in the cellular environment. In this study, we report that both GroEL and its isolated apical domain form amyloid-like fibrils under physiological conditions, and that the fibrillation of the apical domain is accelerated under acidic conditions. We also found, however, that despite its fibrillation propensity, the apical domain exhibits a pronounced inhibitory effect on the fibril growth of β(2)-microglobulin. Thus, the analysis of the behaviour of the apical domain reveals how aggregation and chaperone-mediated anti-aggregation processes can be closely related.
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