The intellectual merit of this project is in the use of biophysical and computational tools to examine hypotheses about the mechanism of action of biological activity of amyloid forming and aggregated proteins. The combination of modeling and experiment, biophysical as well as biological characterization, and the use of neuron-like and T cell lines provides one with a multifaceted and unique approach to tackle this important problem.

The broader impacts of this work will enable one to identify key features of the protein- cell interactions that are associated with biological activity and thus pave the way for developing strategies to alter adverse biological responses. It is believed that understanding the relationship between structure, stability, and biological activity may be useful in a variety of applications such as: treatment of disease, the design of biosensors for the detection of toxic proteins, or in any application in which protein aggregation may occur. Results from a previous NSF award have already been modified and used for two consecutive years with great success for one of the laboratory courses in the Bioengineering track at UMBC. Success of this project would lead to further integration of research into both graduate and undergraduate education at UMBC.

Project Start
Project End
Budget Start
2008-10-01
Budget End
2013-09-30
Support Year
Fiscal Year
2008
Total Cost
$367,949
Indirect Cost
Name
University of Maryland Baltimore County
Department
Type
DUNS #
City
Baltimore
State
MD
Country
United States
Zip Code
21250