From Structure, Dynamics, and Assembly of Human Antimicrobial Proteins to Functions: A Chemist’s Perspective

Abstract: Antimicrobial proteins in humans sequester zinc to curtail infection. Although well established as key components of the immune response, the mechanisms of action of these proteins, such as S100A12, in the inflammatory pathway are not well understood. In this talk, I will present our work on biophysical characterization of S100A12 using NMR spectroscopy, together with cellular studies evaluating the origin of inflammatory signals triggered by the protein. In particular, I will focus on the roles of Ca(II) and Zn(II) toward modulating the structure and internal dynamics of S100A12 that afford its biological functions.
Based on our studies, we propose a generalized model describing the molecular events that enable S100A12 and related antimicrobial proteins to regulate infection and inflammation during immune response.