RESEARCH ARTICLE
Biotinylated Microbubbles Targeted to Amyloid
Arlymae Rand1, Gregory Gilman2, Dennis J. O’Kane1, Marek Belohlavek3, *
Article Information
Identifiers and Pagination:
Year: 2008Volume: 1
First Page: 75
Last Page: 78
Publisher Id: TOCCHEMJ-1-75
DOI: 10.2174/1874241600801010075
Article History:
Received Date: 14/7/2008Revision 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.
Abstract
Background:
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.
Methods:
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).
Results:
Microbubbles with a protein shell were bound to amyloid by utilizing the affinity of SAP for amyloid and biotinavidin interactions.
Conclusion:
We introduce microbubbles specifically targeted to amyloid deposits and intended as future mediators of ultrasound detection of amyloid deposits and amyloid-selective drug delivery.