Modification of Antimicrobial Agent Compound by Alterations in Structure and Functionality Via Amino Acid Coupling

Presentation Type

Poster/Portfolio

Presenter Major(s)

Biomedical Sciences

Mentor Information

Laurie Witucki

Department

Chemistry

Start Date

11-4-2012 9:00 AM

Keywords

Health

Abstract

The parent compound WS.11.67 is a modified peptide analog developed by our lab to probe the specificity of Focal Adhesion Kinase (FAK), an enzyme found to be up-regulated in many cancer cases, such as breast and prostate cancers. The focus of our lab has been the modification of the compounds tyrosine residue through peptide coupling with select amino acids. Protected tryptophan residues were coupled through amid bond formation to WS.11.67 using N,N'-Dicyclohexylcarbodiimide (DCC), O-(Cyano(ethoxycarbonyl)methylenamino)-1,1,3,3-tetramethyluronium tetrafluoroborate (TOTU), or a ring closure mechanism, confirmed by 1H-NMR, 13C-NMR and Inferred Spectroscopy. These compounds and other future products will be tested for their ability to maintain similar antimicrobial potential while decreasing its affinity for Human Serum Protein compared to binding WS.11.67.

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Apr 11th, 9:00 AM

Modification of Antimicrobial Agent Compound by Alterations in Structure and Functionality Via Amino Acid Coupling

The parent compound WS.11.67 is a modified peptide analog developed by our lab to probe the specificity of Focal Adhesion Kinase (FAK), an enzyme found to be up-regulated in many cancer cases, such as breast and prostate cancers. The focus of our lab has been the modification of the compounds tyrosine residue through peptide coupling with select amino acids. Protected tryptophan residues were coupled through amid bond formation to WS.11.67 using N,N'-Dicyclohexylcarbodiimide (DCC), O-(Cyano(ethoxycarbonyl)methylenamino)-1,1,3,3-tetramethyluronium tetrafluoroborate (TOTU), or a ring closure mechanism, confirmed by 1H-NMR, 13C-NMR and Inferred Spectroscopy. These compounds and other future products will be tested for their ability to maintain similar antimicrobial potential while decreasing its affinity for Human Serum Protein compared to binding WS.11.67.