Biotinylated Microbubbles Targeted to Amyloid



Arlymae Rand1, Gregory Gilman2, Dennis J. O’Kane1, Marek Belohlavek3, *
1 Mayo Clinic, Rochester, Minnesota
2 Kardia Health Systems, Rochester, Minnesota and
3 Mayo Clinic, Scottsdale, Arizona, USA


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© 2008 Rand et al;

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.

* Address correspondence to this author at the Mayo Clinic Arizona, Johnson Research Building 3-361, 13400 E. Shea Boulevard, Scottsdale, Arizona 85259, USA; Tel: 480-301-6694 (office), 480-301-6870 (admin. assistant); Fax: 480-301-9162; E-mail: belohlavek.marek@mayo.edu


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.

Keywords: Targeted microbubbles, amyloid.