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Published on: December 13, 2016
Controlled aggregation of ferritin to modulate MRI relaxivity
Kevin M Bennett1, Erik M Shapiro, Christopher H Sotak
1Laboratory of Functional and Molecular Imaging, National Institutes of Neurological Disease and Stroke, National Institutes of Health, Bethesda, MD 20892-1065, USA.
Biophysical Journal
|March 11, 2008
Summary
Researchers enhanced ferritin's MRI contrast by aggregating it. This aggregation, achieved through cross-linking or binding to actin, significantly increased ferritin's relaxivity, making it a more effective reporter for magnetic resonance imaging.
Area of Science:
- Biophysics
- Biochemistry
- Biotechnology
Background:
- Ferritin, an iron storage protein, is a potential MRI contrast agent.
- Current limitations include low T2 relaxivity (R2) requiring high expression levels for detection.
- Aggregation is a strategy to enhance MRI contrast agent performance.
Purpose of the Study:
- To investigate if ferritin aggregation can alter its relaxivity for improved MRI applications.
- To determine the effects of aggregate size and spacing on R2 relaxivity.
- To explore biologically relevant methods for ferritin aggregation.
Main Methods:
- Computer simulations to model relaxivity changes with aggregation.
- In vitro experiments involving chemical cross-linking of ferritin.
- In vitro polymerization of ferritin with actin filaments.
Main Results:
- Computer modeling suggested optimal ferritin spacing of 100-200 nm for increased R2.
- Chemical cross-linking increased R2 by 70% compared to controls.
- Ferritin-actin polymerization increased R2 by 20%, with further increases upon altering spacing.
Conclusions:
- Ferritin aggregation can significantly modulate its R2 relaxivity.
- Controlled aggregation, particularly with cytoskeletal elements, offers a strategy for developing functional MRI reporter genes.
- This approach could enhance sensitivity and utility of ferritin in magnetic resonance imaging.
