TY  - JOUR
AU  - Sun, Xun
AU  - Saha, Debasis
AU  - Wang, Xue
AU  - Mörman, Cecilia
AU  - Sternke-Hoffmann, Rebecca
AU  - Gerez, Juan Atilio
AU  - Herranz-Trillo, Fátima
AU  - Riek, Roland
AU  - Zheng, Wenwei
AU  - Luo, Jinghui
TI  - Spermine modulation of Alzheimer’s Tau and Parkinson’s α-synuclein: implications for biomolecular condensation and neurodegeneration
JO  - Nature Communications
VL  - 16
IS  - 1
SN  - 2041-1723
CY  - [London]
PB  - Springer Nature
M1  - PUBDB-2026-00447
SP  - 10239
PY  - 2025
AB  - Spermine, a pivotal player in biomolecular condensation and diverse cellular processes, has emerged as a focus of investigation in aging, neurodegeneration, and other diseases. Despite its significance, the mechanistic details of spermine remain incompletely understood. Here, we describe the distinct modulation by spermine on Alzheimer’s Tau and Parkinson’s α-synuclein, elucidating their condensation behaviors in vitro and in vivo. Using biophysical techniques including time-resolved SAXS and NMR, we trace electrostatically driven transitions from atomic-scale conformational changes to mesoscopic structures. Notably, spermine extends lifespan, ameliorates movement deficits, and restores mitochondrial function in C. elegans models expressing Tau and α-synuclein. Acting as a molecular glue, spermine orchestrates in vivo condensation of α-synuclein, influences condensate mobility, and promotes degradation via autophagy, specifically through autophagosome expansion. This study unveils the interplay between spermine, protein condensation, and functional outcomes, advancing our understanding of neurodegenerative diseases and paving the way for therapeutic development.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1038/s41467-025-65426-3
UR  - https://bib-pubdb1.desy.de/record/644614
ER  -