Presentation Title

Determination of Binding Constants between Indolicidin and its Derivatives and Sphingomyelin

Format of Presentation

Poster to be presented Friday March 31, 2017

Abstract

The ability of certain peptides to display antimicrobial activity has made them a research interest surrounding drug design. The antimicrobial peptide (AMP), indolicidin, was originally isolated from bovine neutrophils. Peptide 45 and peptide 5 are derivatives of indolicidin that have been previously studied for penetrating bacterial cells and showed little hemolytic activity against red blood cells (RBCs). One of the major components of the red blood cell membrane is sphingomyelin. In this study, Frontal Analysis Capillary Electrophoresis (FACE) is used to determine the binding constants between indolicidin and its derivatives and varying concentrations of sphingomyelin. Two buffers are created for this method and the method is tested using previously optimized conditions and re-optimized if necessary. By using FACE, the extent that the derivative binds to sphingomyelin will be determined and therefore the extent of hemolytic activity or lack thereof can be inferred. This research intends to show that the derivatives of indolicidin would not be harmful to human RBCs and consequently will demonstrate the efficacy of the derivatives as a potential drug targets to kill drug-resistant bacteria.

Department

Chemistry

Faculty Advisor

Heidi Huttunen-Hennelly

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Determination of Binding Constants between Indolicidin and its Derivatives and Sphingomyelin

The ability of certain peptides to display antimicrobial activity has made them a research interest surrounding drug design. The antimicrobial peptide (AMP), indolicidin, was originally isolated from bovine neutrophils. Peptide 45 and peptide 5 are derivatives of indolicidin that have been previously studied for penetrating bacterial cells and showed little hemolytic activity against red blood cells (RBCs). One of the major components of the red blood cell membrane is sphingomyelin. In this study, Frontal Analysis Capillary Electrophoresis (FACE) is used to determine the binding constants between indolicidin and its derivatives and varying concentrations of sphingomyelin. Two buffers are created for this method and the method is tested using previously optimized conditions and re-optimized if necessary. By using FACE, the extent that the derivative binds to sphingomyelin will be determined and therefore the extent of hemolytic activity or lack thereof can be inferred. This research intends to show that the derivatives of indolicidin would not be harmful to human RBCs and consequently will demonstrate the efficacy of the derivatives as a potential drug targets to kill drug-resistant bacteria.