title: Following the aggregation of human prion protein on Au(111) surface in real-time.
abstract: Aggregations of human prion protein (23-231) were monitored by atomic force microscopy in real-time under pH 4. Prion dimers and trimers were determined as the basic units by AFM images and simulated structures. Aggregates aligned with the herringbone structures of an Au(111) reconstructed surface via Au-S bonds as the first layer, while the second layer was formed by non-covalent interactions.
authors.affiliation: Single Molecule Study Laboratory, Faculty of Engineering and Nanoscale Science and Engineering Center, University of Georgia, Athens, GA 30602, USA. bxu@engr.uga.edu.
authors.forename: Bin
authors.initials: B
authors.lastname: Wang
authors.forename: Cunlan
authors.initials: C
authors.lastname: Guo
authors.forename: Zhichao
authors.initials: Z
authors.lastname: Lou
authors.forename: Bingqian
authors.initials: B
authors.lastname: Xu
mesh_terms: D006046:Gold / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D018625:Microscopy, Atomic Force; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011328:Prions / Q000737:chemistry*; D066329:Protein Aggregates; D011487:Protein Conformation; D013499:Surface Properties; D013997:Time Factors
chemical_list: D010446:Peptide Fragments; D011328:Prions; D066329:Protein Aggregates; C428437:prion protein (23-231); D006046:Gold