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Updated: May 16, 2026

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy
Published on: November 30, 2018
Facile methodology for monitoring amyloid-β fibrillization
1Department of Chemistry, Department of Bioengineering, and Smalley Institute for Nanoscale Science and Technology, Rice University, 6100 South Main Street, Houston, Texas 77005, United States.
Abstract:
Amyloid-β (Aβ) is a peptide fragment that is prone to aggregate into large fibrils under physiological conditions. Many techniques have been developed to quickly monitor the transition from a primarily monomeric peptide into fibrils. Here we propose a novel method for both incubating and monitoring changes in Aβ aggregation by using modified NMR tubes, a microtube thermoshaker, and a fluorescence or UV-vis spectrometer. These NMR tubes are thin and cylindrical, which allows efficient heat transfer and orbital shaking. Our results demonstrate that our technique is both reliable and expedient when tracking Aβ fibrillization using fluorescence or turbidity assays, which presents an alternative for laboratories without specialized equipment for incubating peptide.
