Self-assembly of bacterial amyloid protein nanomaterials on solid surfaces

Date
2018
Advisor
Instructor
Source Title
Journal of Colloid and Interface Science
Print ISSN
0021-9797
Electronic ISSN
1095-7103
Publisher
Academic Press
Volume
520
Issue
Pages
145 - 154
Language
English
Type
Article
Journal Title
Journal ISSN
Volume Title
Abstract

Hypothesis: Amyloid-forming biofilm proteins of Escherichia coli, namely CsgA and CsgB, can form self-assembled nanofibers on solid surfaces. These proteins can be programmed to form bio-nanomaterials for functional applications. Experiments: In this study, the assembly of the CsgA and CsgB protein on solid surfaces was investigated in real time using a quartz crystal microbalance instrument with dissipation monitoring. The assembly kinetics of the CsgA and CsgB proteins in various settings on solid surfaces were investigated. Protein nanowires were investigated using electron microscopy. Findings: CsgA protein polymers and CsgB-added CsgA polymers form densely packed biofilm on gold surfaces, whereas CsgB polymers and CsgA-added CsgB polymers form biofilms with high water-holding capacity according to the dissipation data. Electron microscopy images of nanofibers grown on gold surfaces showed that CsgA and CsgB polymers include thicker nanofibers compared to the nanofibers formed by CsgA-CsgB protein combinations. The resulting nano/microstructures were found to have strong fluorescence signals in aqueous environments and in chloroform while conserving the protein nanowire network.

Course
Other identifiers
Book Title
Keywords
Amyloids, Bacterial biofilm proteins, Curli, Nanomaterials
Citation
Published Version (Please cite this version)