Characteristics of surface adsorption of leucine enkephalin on fused silica

CHED 970

Nicole M. Litzie, litzie@sonoma.edu, Meng-Chih Su, sum@sonoma.edu, and Jennifer Whiles Lillig, Jennifer.Whiles@sonoma.edu. Department of Chemistry, Sonoma State University, Rohnert Park, CA 94928
Leucine enkephalin is a peptide found in the human brain that may function as a natural painkiller. Most similar peptides require interaction with membrane-bound receptors in order to function. Previous structural studies of this peptide using attenuated total internal reflection (ATR-IR) and solution IR seem to show contradictory results. This research project seeks to fully characterize the surface adsorption of the protein, to compare its optical absorbance and emission activities on a fused silica glass surface to those of the protein in solution. The affinity of the protein to the surface and its denaturation by pH variation will be measured using ATR spectroscopy in the UV region. In the first study of its kind at SSU, leucine enkephalin conformational changes and biological activity in an environment closely related to its natural one will be examined, with applicability to advance work in disease prevention and treatment, biotechnology, and more.