Biotinylated Microbubbles Targeted to Amyloid
Arlymae Rand1, Gregory Gilman2, Dennis J. O’Kane1, Marek Belohlavek3, *
Identifiers and Pagination:Year: 2008
First Page: 75
Last Page: 78
Publisher Id: TOCCHEMJ-1-75
Article History:Received Date: 14/7/2008
Revision Received Date: 5/09/2008
Acceptance Date: 15/10/2008
Electronic publication date: 11/11/2008
Collection year: 2008
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Ultrasonography uses microbubbles for enhanced imaging. We created microbubbles that have preferential adherence to amyloid protein by utilizing the affinity of serum amyloid component P (SAP) to amyloid along with avidin-biotin interactions.
Biotin-labeled albumin was incorporated into the albumin shell of fluorocarbon gas-filled bubbles. The bubble was attached through a bridge with biotin incorporated into the shell of the bubble and incubated with avidin-labeled SAP which was pre-bound to SA (“synthetic amyloid”). This resulted in a bubble targeted to amyloid. The bubbles were evaluated using fluorescent microscopy and fluorescence-activated cell sorting (FACS).
Microbubbles with a protein shell were bound to amyloid by utilizing the affinity of SAP for amyloid and biotinavidin interactions.
We introduce microbubbles specifically targeted to amyloid deposits and intended as future mediators of ultrasound detection of amyloid deposits and amyloid-selective drug delivery.