Apr 21, 2014

Characterization of amyloid β fibril formation under microgravity conditions

BioRxiv : the Preprint Server for Biology
Yuval ElhanatiKoichi Kato

Abstract

Amyloid fibrils are self-assembled and ordered proteinaceous supramolecules structurally characterized by the cross-β spine. Amyloid formation is known to be related to various diseases typified by neurogenerative disorders and involved in a variety of functional roles. Whereas common mechanisms for amyloid formation have been postulated across diverse systems, the mesoscopic morphology of the fibrils is significantly affected by the type of solution condition in which it grows. Amyloid formation is also thought to share a phenomenological similarity with protein crystallization. While many studies have demonstrated the effect of gravity on protein crystallization, its effect on amyloid formation has not been reported. In this study, we conducted an experiment at the International Space Station (ISS) to characterize fibril formation of 40-residue amyloid β (Aβ(1-40)) under microgravity conditions. Our comparative analyses revealed that the Aβ(1-40) fibrilization progresses much more slowly on the ISS than on the ground, similarly to protein crystallization. Furthermore, microgravity promoted the formation of distinct morphologies of Aβ(1-40) fibrils. Our findings demonstrate that the ISS provides an ideal experimental environme...Continue Reading

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Mentioned in this Paper

Immune System
T-Lymphocyte
Immune Effector Cell
Recombination, Genetic
Donor Person
Receptors, Immunologic
Public Entity
T-Cell Receptor
Analysis
Entire Immune System

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