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 (Aβ) involved in Alzheimer's disease (AD), a neurodegenerative disease where unnaturally folded Aβ 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 Aβ at different stages of aggregation allow both, noninvasive exploration and dissolution of molecular aggregates. © 2006 American Chemical Society.