| |
Lisa M. Miller, Ph.D.
Biophysicist, Brookhaven National Laboratory and
Adjunct Assistant Professor, Department of Biomedical Engineering, Stony
Brook University.
Funding through the National Institutes of Health - National Institute
of General Medical Sciences and the U.S. Department of Energy - Basic
Energy Sciences Division.
Figure 1. The combination of infrared
imaging (blue), x-ray imaging (red), and epifluorescence imaging
(green) are used to correlate the location of the misfolded
Abeta protein and zinc accumulation in Alzheimer’s disease. |
|
The focus of our laboratory is on the study of the chemical makeup of
tissue in disease using high-resolution infrared and x-ray imaging at
Brookhaven's National Synchrotron Light Source. We have two primary research
areas: (1) examination of the chemical composition of bone tissue in diseases
such as osteoarthritis and osteoporosis, and (2) correlation of metal
ion content and protein structure in brain tissue in protein-folding diseases
such as Alzheimer's disease and scrapie. In bone disease, there is often
an imbalance between the processes of bone production and resorption,
which results in an increase (as in osteoarthritis) or decrease (as in
osteoporosis) in bone density. However, it is unclear whether the composition
of bone is affected. Thus, infrared imaging and micro-spectroscopy are
used to determine parameters such as protein and mineral content, structure,
and environment. With this information, a chemical picture of how bone
composition affects the mechanical and structural properties of bone can
be developed. In many protein-folding diseases, proteins that normally
occur in the brain are found to misfold and aggregate, causing neurological
damage. These protein aggregates are often associated with high metal
content in the brain. For example, high concentrations of zinc have been
associated with amyloid plaques in Alzheimer's disease. Using synchrotron
x-ray and infrared imaging, the metal ions and protein aggregates can
be imaged and correlated. These findings will help to determine how the
accumulation of metal ions in the brain is associated with protein misfolding.
Students with a bioengineering and/or chemical/physical sciences background
will be introduced to the use of synchrotron-based spectroscopic imaging
tools for examination of the composition of tissue in control and diseased
states. The projects involve the use of animal models of Alzheimer’s
disease and bone diseases such as osteoporosis and osteoarthritis. Trainees
will learn to prepare tissues for spectroscopic analysis and will have
the opportunity to work on the x-ray and/or infrared microscopes at the
National Synchrotron Light Source. Classical biochemical and spectroscopic
experiments will complement the microscopic data. Data analysis and image
generation will be taught, including statistical analysis and interpretation.
A fundamental understanding of each technique will be learned, emphasizing
their complementarity, and also their relationship to information obtained
by other imaging modalities such as CT, MRI, and PET.
Contact Information
email: lmiller@bnl.gov
url:
back to top
|
|
