The Open Clinical Biochemistry Journal

2008, 1 : 75-78
Published online 2008 November 11. DOI: 10.2174/1874241600801010075
Publisher ID: TOCCHEMJ-1-75

Biotinylated Microbubbles Targeted to Amyloid

Arlymae Rand , Gregory Gilman , Dennis J. O’Kane and Marek Belohlavek
Mayo Clinic Arizona, Johnson Research Building 3-361, 13400 E. Shea Boulevard, Scottsdale, Arizona 85259, USA.

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.