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Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State

Amyloid Formation in Nanoliter Droplets

by 1,2,†, 3,†, 4, 5,* and 1,2,*
Department of Biotechnology and Bioinformatics, Korea University, Sejong 30019, Korea
Interdisciplinary Graduate Program for Artificial Intelligence Smart Convergence Technology, Korea University, Sejong 30019, Korea
Department of Electrical Engineering, Korea National University of Transportation, Chungju 27469, Korea
Nick Holonyak Jr. Micro and Nanotechnology Laboratory, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA
Department of Biomechatronic Engineering, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon 16419, Korea
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Vytautas Smirnovas
Int. J. Mol. Sci. 2022, 23(10), 5480;
Received: 30 March 2022 / Revised: 11 May 2022 / Accepted: 12 May 2022 / Published: 13 May 2022
(This article belongs to the Special Issue The Role of Environment in Amyloid Aggregation 2.0)
Processes that monitor the nucleation of amyloids and characterize the formation of amyloid fibrils are vital to medicine and pharmacology. In this study, we observe the nucleation and formation of lysozyme amyloid fibrils using a facile microfluidic system to generate nanoliter droplets that can control the flow rate and movement of monomer-in-oil emulsion droplets in a T-junction microchannel. Using a fluorescence assay, we monitor the nucleation and growth process of amyloids based on the volume of droplets. Using the microfluidic system, we demonstrate that the lag phase, which is vital to amyloid nucleation and growth, is reduced at a lower droplet volume. Furthermore, we report a peculiar phenomenon of high amyloid formation at the edge of a bullet-shaped droplet, which is likely due to the high local monomer concentration. Moreover, we discovered that amyloid fibrils synthesized in the nanoliter droplets are shorter and thicker than fibrils synthesized from a bulk solution via the conventional heating method. Herein, a facile procedure to observe and characterize the nucleation and growth of amyloid fibrils using nanoliter droplets is presented, which is beneficial for investigating new features of amyloid fibril formation as an unconventional synthetic method for amyloid fibrils. View Full-Text
Keywords: lysozyme; amyloid formation; nanoliter droplet; fluorescence assay; atomic force microscopy; polymorphism lysozyme; amyloid formation; nanoliter droplet; fluorescence assay; atomic force microscopy; polymorphism
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MDPI and ACS Style

Cheong, D.Y.; Lee, W.; Park, I.; Park, J.; Lee, G. Amyloid Formation in Nanoliter Droplets. Int. J. Mol. Sci. 2022, 23, 5480.

AMA Style

Cheong DY, Lee W, Park I, Park J, Lee G. Amyloid Formation in Nanoliter Droplets. International Journal of Molecular Sciences. 2022; 23(10):5480.

Chicago/Turabian Style

Cheong, Da Y., Wonseok Lee, Insu Park, Jinsung Park, and Gyudo Lee. 2022. "Amyloid Formation in Nanoliter Droplets" International Journal of Molecular Sciences 23, no. 10: 5480.

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