Issue 36, 2023

Magnetic PiezoBOTs: a microrobotic approach for targeted amyloid protein dissociation

Abstract

Piezoelectric nanomaterials have become increasingly popular in the field of biomedical applications due to their high biocompatibility and ultrasound-mediated piezocatalytic properties. In addition, the ability of these nanomaterials to disaggregate amyloid proteins, which are responsible for a range of diseases resulting from the accumulation of these proteins in body tissues and organs, has recently gained considerable attention. However, the use of nanoparticles in biomedicine poses significant challenges, including targeting and uncontrolled aggregation. To address these limitations, our study proposes to load these functional nanomaterials on a multifunctional mobile microrobot (PiezoBOT). This microrobot is designed by coating magnetic and piezoelectric barium titanate nanoparticles on helical biotemplates, allowing for the combination of magnetic navigation and ultrasound-mediated piezoelectric effects to target amyloid disaggregation. Our findings demonstrate that acoustically actuated PiezoBOTs can effectively reduce the size of aggregated amyloid proteins by over 80% in less than 10 minutes by shortening and dissociating constituent amyloid fibrils. Moreover, the PiezoBOTs can be easily magnetically manipulated to actuate the piezocatalytic nanoparticles to specific amyloidosis-affected tissues or organs, minimizing side effects. These biocompatible PiezoBOTs offer a promising non-invasive therapeutic approach for amyloidosis diseases by targeting and breaking down protein aggregates at specific organ or tissue sites.

Graphical abstract: Magnetic PiezoBOTs: a microrobotic approach for targeted amyloid protein dissociation

Supplementary files

Article information

Article type
Paper
Submitted
25 mai 2023
Accepted
17 aug 2023
First published
18 aug 2023
This article is Open Access
Creative Commons BY-NC license

Nanoscale, 2023,15, 14800-14808

Magnetic PiezoBOTs: a microrobotic approach for targeted amyloid protein dissociation

S. Ning, R. Sanchis-Gual, C. Franco, P. D. Wendel-Garcia, H. Ye, A. Veciana, Q. Tang, S. Sevim, L. Hertle, J. Llacer-Wintle, X. Qin, C. Zhu, J. Cai, X. Chen, B. J. Nelson, J. Puigmartí-Luis and S. Pané, Nanoscale, 2023, 15, 14800 DOI: 10.1039/D3NR02418K

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party commercial publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements