Event Title

Synthesis of Novel Peptides as Focal Adhesion Kinase Inhibitors

Presentation Type

Poster/Portfolio

Presenter Major(s)

Biomedical Sciences, Cell and Molecular Biology

Mentor Information

Laurie Witucki

Department

Chemistry

Location

Kirkhof Center KC86

Start Date

11-4-2012 9:00 AM

Keywords

Health, Life Science

Abstract

Focal Adhesion Kinase (FAK) is a protein kinase involved in signal transduction at cellular focal adhesions. Protein kinases function by altering a substrate via phosphorylation, thereby altering the substrates functionality, often turning it on or off. By targeting FAK for inhibition, it may be possible to prevent the signal transduction of cancerous cells responsible for releasing cell anchorage and metastasizing. This investigation involved designing novel peptide substrates that mimick the protein CASp130, a reported in vivo substrate. The two peptides synthesized were DH-1: DVYDVPKKK and DH-2: DIYDVPKKK. Each peptide contained a string of 6 amino acids isolated from the CASp130 protein attached to a polylysine tail required for functionality of the phosphorylation assay. The peptides were synthesized using solid phase peptide synthesis methods, both manual and automated.

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Apr 11th, 9:00 AM

Synthesis of Novel Peptides as Focal Adhesion Kinase Inhibitors

Kirkhof Center KC86

Focal Adhesion Kinase (FAK) is a protein kinase involved in signal transduction at cellular focal adhesions. Protein kinases function by altering a substrate via phosphorylation, thereby altering the substrates functionality, often turning it on or off. By targeting FAK for inhibition, it may be possible to prevent the signal transduction of cancerous cells responsible for releasing cell anchorage and metastasizing. This investigation involved designing novel peptide substrates that mimick the protein CASp130, a reported in vivo substrate. The two peptides synthesized were DH-1: DVYDVPKKK and DH-2: DIYDVPKKK. Each peptide contained a string of 6 amino acids isolated from the CASp130 protein attached to a polylysine tail required for functionality of the phosphorylation assay. The peptides were synthesized using solid phase peptide synthesis methods, both manual and automated.