Honors Theses

Date of Award

2012

Document Type

Undergraduate Thesis

Department

Chemistry and Biochemistry

First Advisor

Susan Pedigo

Relational Format

article

Abstract

Cadherins are calcium-dependent cell adhesion molecules whose general structure is characterized by three regions: a conserved carboxy-terminal cytoplasmic region, a transmembrane segment and an extracellular region that binds calcium. Cadherins mediate cell to cell adhesion by the formation of homophilic dimers between these extracellular regions, during which one cadherin molecule interacts with another cadherin molecule of the same type. The adhesive interface is a strand-crossover structure between two protomers from adjacent cells. The PA-strand detaches from its own protomer and crosses over to dock a critical tryptophan residue in a hydrophobic partner protomer. Disruption of the formation of the adhesive dimer is of great interest as a chemotherapeutic strategy for cancer metastasis. The histidine-alanine-valine (HAV) peptide is a motif in cadherin that may have a role in dimerization and overall cell adhesion. It causes a decrease in synapse duration in vivo. Experiments reported here were designed to test whether we can detect an effect of the HAV peptide on dimerization using a simple chromatographic assay developed in our laboratory. Results were negative in that the peptide does not disassemble the adhesive dimer in our chromatographic assay.

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