[한국대학신문 이원지 기자] KAIST (President Lee Kwang-hyung) announced on the 16th that Professor Chan-beom Park’s research team in the Department of Materials Science and Engineering has succeeded in developing low-frequency magnetic field-responsive nanoparticles.
Using this, the beta-amyloid peptide (amino acid compound) aggregate that causes Alzheimer’s disease can be decomposed with a magnetic field.
This research, in which KAIST’s Department of Materials Science and Engineering, Ph.D. Jang Jin-hyeong participated as the first author, was published in an international scientific journal. was published on the 13th. The title of the paper is ‘Magnetoelectric dissociation of Alzheimer’s β-amyloid aggregates’.
Magnetoelectric materials have properties that combine magnetism and electricity, and are a core material constituting various electronic devices such as spintronics devices and transducers. However, magnetoelectric materials have limitations in improving their performance due to the electrostatic interaction of protons (spin-orbit interaction) that interferes with the rotation and orbital motion of electrons in atoms.
The research team developed heterogeneous magnetoelectric nanoparticles by bonding cobalt ferrite and bismuth ferrite, which are a type of magnetoelectric material, mainly used in semiconductor and battery fields, in a core-shell structure. did. Through the uniform bonding of different magnetoelectric materials, a magneto-piezoelectric effect that responds to low-frequency magnetic fields at their interface might be induced.
In particular, the research team paid attention to the phenomenon that nanoparticles do not emit heat when they generate charge carriers in response to low-frequency magnetic fields. The magnetic field can penetrate brain tissue without damage and its medical safety has already been verified by being used in Magnetic Resonance Imaging (MRI).
When a low-frequency magnetic field was applied to the nanoparticles developed by the research team, the research team observed that beta-amyloid peptide was oxidized by weakening the binding force of the aggregate and decomposed, and neurotoxicity was also neutralized.
Amyloid aggregates are commonly observed in various neurodegenerative diseases such as Alzheimer’s disease and have been known to be difficult to decompose because they have a very stable protein secondary structure through regular hydrogen bonding.
Professor Park said, “Low-frequency magnetic field-responsive nanomaterials have low toxicity and have potential to be expanded to medical fields because they can efficiently decompose amyloid aggregates by reacting with magnetic fields.” Animal experiments using
Meanwhile, this research was carried out with support from the Ministry of Science and ICT Leader Researcher Support Project (Creative Research).
