Gold nanoparticles for selective and remote heating of β-amyloid protein aggregates

Neus G. Bastus, Marcelo J. Kogan, Roger Amigo, Dolors Grillo-Bosch, Eyleen Araya, Antonio Turiel, Amilcar Labarta, Ernest Giralt, Victor F. Puntes

Resultado de la investigación: Contribución a una revistaArtículo

41 Citas (Scopus)

Resumen

Nanoparticles can be made to respond resonantly to a time-varying electromagnetic field with advantageous results related to the transfer of energy from the exciting field to the nanoparticles. The surface of each particle can be heated up, this heat being transmitted into the immediately surrounding tissue. This enables their use as hyperthermia agents delivering toxic amounts of thermal energy to targeted bodies such as tumours. Heating of nanoparticles in a magnetic field is mainly due to inductive coupling (via eddy currents), and in the case of magnetic particles, loss processes during the reorientation of the magnetization (hysteresis losses) or frictional losses (relaxational losses) if the particle can rotate in an environment of sufficiently low viscosity. We use this method to apply heat locally and remotely, dissolving toxic protein deposits of Aβ1-42 (amyloid deposits) via the combined use of weak microwave fields and gold nanoparticles (AuNP) without any bulk heating. This method can be extended to a number of systems where it may be desirable to remove proteins and other aggregates involved in different pathologies.

Idioma originalInglés
Páginas (desde-hasta)1236-1240
Número de páginas5
PublicaciónMaterials Science and Engineering C
Volumen27
N.º5-8 SPEC. ISS.
DOI
EstadoPublicada - 1 sep 2007

Áreas temáticas de ASJC Scopus

  • Biomateriales

Huella Profundice en los temas de investigación de 'Gold nanoparticles for selective and remote heating of β-amyloid protein aggregates'. En conjunto forman una huella única.

  • Citar esto

    Bastus, N. G., Kogan, M. J., Amigo, R., Grillo-Bosch, D., Araya, E., Turiel, A., Labarta, A., Giralt, E., & Puntes, V. F. (2007). Gold nanoparticles for selective and remote heating of β-amyloid protein aggregates. Materials Science and Engineering C, 27(5-8 SPEC. ISS.), 1236-1240. https://doi.org/10.1016/j.msec.2006.08.003