Nanoparticle-mediated local and remote manipulation of protein aggregation.
The local heat delivered by metallic nanoparticles selectively attached to their target can be used as a molecular surgery to safely remove toxic and clogging aggregates. We apply this principle to protein aggregates, in particular to the amyloid beta protein (Abeta) involved in Alzheimer's disease (AD), a neurodegenerative disease where unnaturally folded Abeta proteins self-assemble and deposit forming amyloid fibrils and plaques. We show the possibility to remotely redissolve these deposits and to interfere with their growth, using the local heat dissipated by gold nanoparticles (AuNP) selectively attached to the aggregates and irradiated with low gigahertz electromagnetic fields. Simultaneous tagging and manipulation by AuNP of Abeta at different stages of aggregation allow both, noninvasive exploration and dissolution of molecular aggregates.
Kogan
Marcelo J
MJ
Institut de Recerca Biomèdica de Barcelona, Parc Científic de Barcelona-UB, Spain. mkogan@ciq.uchile.cl
Bastus
Neus G
NG
Amigo
Roger
R
Grillo-Bosch
Dolors
D
Araya
Eyleen
E
Turiel
Antonio
A
Labarta
Amilcar
A
Giralt
Ernest
E
Puntes
Victor F
VF
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000528:radiation effects; D019281:Dimerization; D004574:Electromagnetic Fields; D017979:Gold Colloid / Q000737:chemistry* / Q000528:radiation effects; D006361:Heating; D046529:Microscopy, Electron, Transmission; D008872:Microwaves; D049329:Nanostructures; D010446:Peptide Fragments / Q000737:chemistry* / Q000528:radiation effects
D016229:Amyloid beta-Peptides; D017979:Gold Colloid; D010446:Peptide Fragments; C075222:amyloid beta-protein (1-42)