Impact of microgravity on the fibrillization kinetics and structure of amyloid beta peptide

Abstract

Amyloid beta (Aβ) is a 38–42 residue peptide that is implicated in Alzheimer's disease (AD). The undesirable conversion of the soluble Aβ monomers into oligomers and fibrils leads to loss of neuronal cell functions and disruption of cellular transport and signaling. Studying the behavior of Aβ in microgravity conditions is essential to assess the risk of protein misfolding and the subsequent risk of neurodegenerative disease occurrence during long-term manned space missions. In this study, we demonstrate that microgravity fundamentally alters the aggregation process of Aβ(1–40), delaying the fibrillization kinetics and yielding more linear, less polymorphic fibrils with reduced parallel β-sheet content. These findings highlight the potential of microgravity as a tool for investigating the fundamental mechanisms of amyloid fibril formation and its implications for disease processes.