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Updated: Jan 14, 2026
Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Impact of microgravity on the fibrillization kinetics and structure of amyloid beta peptide
Hitendranath Napa Mallikarjuna1, Anagha Manohar1, Narendran Sekar1
1Department of Applied Mechanics and Biomedical Engineering, Indian Institute of Technology Madras, Chennai, India. swathi.s@iitm.ac.in.
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.
Insights
Microgravity slows amyloid beta (Aβ) aggregation, forming less complex fibrils. This research explores protein misfolding risks for astronauts and Alzheimer
Area of Science:
- Neuroscience
- Biochemistry
- Space Medicine
Background:
- Amyloid beta (Aβ) peptides are linked to Alzheimer's disease (AD).
- Protein misfolding and aggregation into fibrils are key pathological features of AD.
- Understanding Aβ behavior in microgravity is crucial for long-term space mission health risks.
Purpose of the Study:
- To investigate the impact of microgravity on amyloid beta (Aβ) aggregation kinetics and fibril morphology.
- To assess the implications of altered Aβ aggregation in spaceflight for neurodegenerative disease risk.
Main Methods:
- Studied the aggregation of Aβ(1-40) under simulated microgravity conditions.
- Analyzed fibrillization kinetics and characterized the resulting fibril structures.
Main Results:
- Microgravity significantly delayed the fibrillization kinetics of Aβ(1-40).
- Fibrils formed in microgravity were more linear and less polymorphic.
- Reduced parallel β-sheet content was observed in microgravity-induced fibrils.
Conclusions:
- Microgravity fundamentally alters amyloid beta aggregation pathways.
- Findings suggest microgravity could be a tool to study amyloid formation mechanisms.
- Altered Aβ aggregation in space may have implications for astronaut neurodegenerative disease risk.
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