The design, synthesis and analysis of high-affinity peptide-peptoid hybrid ligands that bind EVH1 domains & the synthesis of 1-substituted m-terphenyls that seve as N^C^C and O^C^C ligands for use in cyclometallated platinum complexes

Author

Eric J. Dimise, Union College - Schenectady, NY

Date of Award

6-2005

Document Type

Open Access

Degree Name

Bachelor of Science

Department

Chemistry

Language

English

Abstract

Protein-ligand interactions are often at the center of cellular regulatory processes. The Enabled/ vasodilator Stimulated Phosphoprotein Homology 1 (EVH1) domain of the Enabled/ Vasodilator Stimulated Phosphoprotein (Ena/VASP) protein family has been linked to the regulation of the actin cytoskeleton through multiple protein-protein interactions via the recognition of polyproline amino acid sequences. Here, we examine the structural and physicochemical features of the EVH1 domain in an effort to design high affinity peptide-peptoid hybrid ligands that compete with EVH1's natural binding partners. & The unique photophysical properties of aryl, tridentate complexes of platinum have recently led to a surge in ligand design efforts. Here, we outline a facile synthetic route to platinum ligands with N^C^C and O^C^C binding modes, two classes of compounds that have yet to be investigated.

Recommended Citation

Dimise, Eric J., "The design, synthesis and analysis of high-affinity peptide-peptoid hybrid ligands that bind EVH1 domains & the synthesis of 1-substituted m-terphenyls that seve as N^C^C and O^C^C ligands for use in cyclometallated platinum complexes" (2005). Honors Theses. 2091.
https://digitalworks.union.edu/theses/2091