title: Atomic Force Microscopy Characterization of Protein Fibrils Formed by the Amyloidogenic Region of the Bacterial Protein MinE on Mica and a Supported Lipid Bilayer.
abstract: Amyloid fibrils play a crucial role in many human diseases and are found to function in a range of physiological processes from bacteria to human. They have also been gaining importance in nanotechnology applications. Understanding the mechanisms behind amyloid formation can help develop strategies towards the prevention of fibrillation processes or create new technological applications. It is thus essential to observe the structures of amyloids and their self-assembly processes at the nanometer-scale resolution under physiological conditions. In this work, we used highly force-sensitive frequency-modulation atomic force microscopy (FM-AFM) to characterize the fibril structures formed by the N-terminal domain of a bacterial division protein MinE in solution. The approach enables us to investigate the fibril morphology and protofibril organization over time progression and in response to changes in ionic strength, molecular crowding, and upon association with different substrate surfaces. In addition to comparison of the fibril structure and behavior of MinE1-31 under varying conditions, the study also broadens our understanding of the versatile behavior of amyloid-substrate surface interactions.
authors.affiliation: Institute of Physics, Academia Sinica, Taipei, Taiwan.|Department of Materials Science and Engineering, National Tsing Hua University, Hsinchu, Taiwan.
authors.forename: Ya-Ling
authors.initials: YL
authors.lastname: Chiang
authors.affiliation: Institute of Cellular and Organismic Biology, Academia Sinica, Taipei, Taiwan.
authors.forename: Yuan-Chih
authors.initials: YC
authors.lastname: Chang
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
authors.forename: I-Chen
authors.initials: IC
authors.lastname: Chiang
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
authors.forename: Huey-Ming
authors.initials: HM
authors.lastname: Mak
authors.affiliation: Institute of Physics, Academia Sinica, Taipei, Taiwan.|Department of Materials Science and Engineering, National Tsing Hua University, Hsinchu, Taiwan.
authors.forename: Ing-Shouh
authors.initials: IS
authors.lastname: Hwang
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.|Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
authors.forename: Yu-Ling
authors.initials: YL
authors.lastname: Shih
mesh_terms: D000538:Aluminum Silicates / Q000737:chemistry / Q000378:metabolism*; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D018625:Microscopy, Atomic Force / Q000379:methods*; D046529:Microscopy, Electron, Transmission; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D000538:Aluminum Silicates; D000682:Amyloid; D018797:Cell Cycle Proteins; D029968:Escherichia coli Proteins; D008051:Lipid Bilayers; C093548:MinE protein, E coli; D010446:Peptide Fragments; C011934:mica