Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.
Interaction between monomer peptides and seeds is essential for clarifying the fibrillation mechanism of amyloid β (Aβ) peptides. We monitored the deposition reaction of Aβ(1-40) peptides on immobilized seeds grown from Aβ(1-42), which caused formation of oligomers in the early stage. The deposition reaction and fibrillation procedure were monitored throughout by novel total-internal-reflection-fluorescence microscopy with a quartz-crystal microbalance (TIRFM-QCM) system. This system allows simultaneous evaluation of the amount of deposited peptides on the surface seeds by QCM and fibril nucleation and elongation by TIRFM. Most fibrils reached other nuclei, forming the fibril network across the nucleus hubs in a short time. We found a fibril-elongation rate two-orders-of-magnitude higher in an oligomeric cloud than reported values, indicating ultrafast transition of oligomers into fibrils.
Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Hirotsugu
H
Ogi
Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Masahiko
M
Fukukshima
Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Hiroki
H
Hamada
Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Kentaro
K
Noi
Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan.
Masahiko
M
Hirao
Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
Hisashi
H
Yagi
Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka 565-0871, Japan.
Yuji
Y
Goto
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D052160:Benzothiazoles; D005427:Flocculation; D005456:Fluorescent Dyes / Q000737:chemistry; D006801:Humans; D008856:Microscopy, Fluorescence / Q000295:instrumentation / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry*; D066329:Protein Aggregates; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D058525:Quartz Crystal Microbalance Techniques / Q000295:instrumentation / Q000379:methods*; D012996:Solutions; D013844:Thiazoles / Q000737:chemistry
D016229:Amyloid beta-Peptides; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D010446:Peptide Fragments; D066329:Protein Aggregates; D012996:Solutions; D013844:Thiazoles; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42); C009462:thioflavin T