Maurice Smith
“Self-Assembly of a Merlin Peptide”
Maurice Smith, Adrianna Shy, and Bing Xu
Hampton University / Chemistry
Hosted by Xu's Lab
Abstract
Merlin, a tumor suppressing protein, is known to be a control center for the hippo pathway which regulates organ size, cellular proliferation, apoptosis, cellular adhesion, invasion, cellular motility and survival. We took a small amino acid sequence from merlin’s binding domain, added a hydrophobic motif (1-pyrenebutyric acid) through solid phase peptide synthesis (SPPS) and observed the self-assembly of the new peptide. Hydrogelation of this peptide was achieved at various concentrations in water and observed through transmission electron microscopy (TEM). We also used circular dichroism to analyze its secondary structure. Further testing is required to gain a better understanding of the cellular responses through the signaling (hippo) pathway, as the function of merlin is not well defined.
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MRSEC REU