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Article

Bisdemethoxycurcumin, a novel potent polyphenolic compound, effectively inhibits the formation of amyloid aggregates in ALS-associated hSOD1 mutant (L38R).

International journal of biological macromolecules - 1 Dec 2024

Kouhi Zeinab Haghgoo, Seyedalipour Bagher, Hosseinkhani Saman, Chaichi Mohammad Javad

Abstract excerpt

Protein misfolding is a biological process that leads to protein aggregation. Anomalous misfolding and aggregation of human superoxide dismutase (hSOD1) into amyloid aggregates is a characteristic feature of amyotrophic lateral sclerosis (ALS), a neurodegenerative illness. Thus, focusing on the L38R mutant may be a wise decision to comprehend the SOD1 disease process in ALS. We suggest that Bisdemethoxycurcumin...

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PMID: 39461630
DOI: 10.1016/j.ijbiomac.2024.136701

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