- Research Description
Testing human umbilical vein endothelial cells’ (HUVECs) response to functionalized lipid bilayer surfaces. The bilayer surfaces are prepared from peptide-amphiphiles using the Langmuir-Blodgett technique and are created to present a fibronectin-mimetic peptide at the exposed surface. The peptide-amphiphiles used are composed of 2 hydrocarbon tails, a short linker, the commonly-used adhesion amino acid sequence Arginine-Glycine-Aspartic Acid (RGD), a spacer mimicking both distance and hydrophilicy/hydrophobicity of the native protein, and finally the synergy site Proline-Histidine-Serine-Arginine-Asparagine (PHSRN). This peptide is a ligand targeting the α5β1 integrin expressed on the surface many cells, including endothelial cells. This ligand-integrin interaction is important in cell adhesion, which influences cell proliferation and migration, among other processes. Designing a peptide that can closely mimic fibronectin has far-reaching therapeutic effects for both interfacial interactions between biomaterials and the body, as well as targeted drug delivery.
B.S. Chemical Engineering, University of Notre Dame, 2004
M.S. Biomedical Engineering, University of Minnesota, 2007
- Degree Attained
- M.S. BME 2007
- Current Occupation
- Accenture, USA