Insights in Analytical Electrochemistry Open Access

Metals and immunity: Explorations of a biological hexahistidine site

Joint Event:8^th Annual Congress on Analytical and Bioanalytical Techniques & 14^th International Conference and Exhibition on Pharmaceutical Formulations

August 28-30, 2017 Brussels, Belgium

Elizabeth M Nolan

Massachusetts Institute of Technology, USA

Keynote: Insights Anal Electrochem

Abstract:

Metal-sequestering innate immune proteins participate in the host/pathogen interaction. The S100 protein family includes calprotectin (S100A8/S100A9), psoriasin (S100A7), and S100A12, and these proteins exhibit antimicrobial activity that results from their ability to chelate transition metals in the extracellular space and thereby reduce the availability of essential metal nutrients to pathogens. Calprotectin is a versatile metal-sequestering protein that can capture a number of divalent firstrow transition metals at an unusual hexahistidine site, whereas psoriasin and S100A12 can selectively deplete zinc. Recent analytical, biochemical, and biophysical studies that address the coordination chemistry and host-defense function of these abundant human proteins with focus on the hexahistidine Zn(II) site of human calprotectin will be presented.

Biography :

Elizabeth M. Nolan is an Associate Professor of Chemistry at MIT. Her research group investigates human host-defense peptides and proteins, and the bioinorganic chemistry the host-microbe interaction and infectious disease.