RUI: Rational design of cysteinyl peptide ligands as chelators of mercury (II)

Winston-Salem State University, Winston Salem NC

Investigators

Abstract

This award in the Chemical Synthesis (SYN) program in the Division of Chemistry supports work by Professors Maria Ngu-Schwemlein, John Merle, and Sayo Fakayode at Winston-Salem State University to carry out fundamental studies on the rational design and synthesis of peptide derived binding agents for the toxic mercury(II) ion. Evaluating the mercury(II) binding affinity of some cysteine-containing peptides will reveal the selectivity and thermodynamic factors that are important in assessing their mode(s) of interaction. Correlations between the chemical structures of some cysteinyl peptide ligands and their binding activity for mercury(II) will be explored by microcalorimetric measurements, and identification of the binding specificity will be conducted by a combination of theoretical calculations and solid state studies. Additionally, the molecular interactions of these compounds with some biological molecules will be monitored by spectroscopic measurements. Selective and effective mercury(II) binding agents are extremely useful for the development of mercury(II) trapping agents for chelation therapy of mercury poisoning. This interdisciplinary research study will enhance the research environment of the chemistry department at Winston-Salem State University in preparing undergraduates, primarily underrepresented groups at this historically black institution, for entry into advanced degree programs and careers in science. This research may also afford a basis for subsequent research in the environmental and health sciences such as the development of microsensors for monitoring toxic and harmful metal ions in environmental and biological samples. Additionally, this research may provide useful peptides for future application in genetically engineered plants that are useful for phytoremediation of mercury(II) pollution in soil or watersheds.