Nanoscale insights into full-length prion protein aggregation on model lipid membranes.
The aggregates of the full-length human recombinant prion protein (PrP) (23-231) on model membranes were investigated by combining the atomic force microscopy (AFM) measurements and theoretical calculations at pH 5.0, showing the great effect of PrP concentration on its supramolecular assemblies on the lipid bilayer.
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
Yangang
Y
Pan
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
Bin
B
Wang
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
Tong
T
Zhang
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
Yanan
Y
Zhang
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, P. R. China.
Hongda
H
Wang
Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
Bingqian
B
Xu
D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D018625:Microscopy, Atomic Force; D062105:Molecular Docking Simulation; D000072002:Prion Proteins / Q000737:chemistry* / Q000378:metabolism; D066329:Protein Aggregates; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
D008051:Lipid Bilayers; D000072002:Prion Proteins; D066329:Protein Aggregates