The molecular characterization of peptide:membrane interactions important in the anit-Listerial activity of bacteriocins.
The re-emergence of bacterial pathogens as a significant threat to public health has lead to an increased awareness of food safety. One of the most common food-born pathogens is Listeria monocytogenes, a bacteria found to contaminate a variety of raw and processed foods including vegetables, meats, and dairy products. Listeria infection can result in a variety of illnesses ranging in severity from fever and nausea to meningitis and fetal miscarriage. In the past decade it has been found that lactic acid bacteria, common food borne bacteria that are non-pathogenic, produce small peptides, termed bacteriocins, that kill Listeria. Work in our lab focuses on understanding the key features of these molecules that allow them to target and kill competing bacteria such as Listeria. We use various methodologies to study these molecular features including spectroscopy (IR, CD, fluorescence), calorimetry, and biological assays. This work can in turn aid in the further development of these molecules as both potent and safe drugs and food preservatives in the endeavor to find new means of fighting and preventing human diseases.
Whiles Lillig, J. "Changing the Focus of the Standard Term-Paper to Encourage Critical Data Analysis in the Upper-Division Chemistry Classroom" J. Chem. Education 85, 1392-1394(2008).
Plesniak, L., Parducho, J., Ziebart, A. Geierstanger, B., Whiles, J., Melacini, G., and Jennings. P. "Orientation and helical conformation of a tissue-specific hunter-killer peptide in micelles." Protein Science 13, 1988-1996 (2004).
J. Whiles, K. Glover, R.R. Vold, and E. Komives. "Methods for studying transmembrane peptides in bicelles: Consequences of hydrophobic mismatch and peptide sequence." J. Mag. Res. 158, 149-156 (2002).
J. Whiles, R. Deems, R.R. Vold, and E. Dennis. "Bicelles in structure-function studies of membrane associated proteins." Biorg. Chem. 30, 431-442 (2002).
K. Glover, J. Whiles, M. Wood, G. Melacini, E. Komives, and R.R. Vold. "Conformational dimorphism and transmembrane orientation of prion protein residues 110-136 in bicelles." Biochem. 40, 13137-13142 (2001).
J. Whiles, R. Brasseur, K. Glover, G. Melacini, E. Komives, and R.R. Vold. "The orientation and effects of mastoparan X on phospholipid bicelles." Biophys. J. 80, 280-293 (2001).
General Chemistry, Structural and Metabolic Biochemistry, Biochemical Methods lab, Research Seminar and Methods, General/Organic/Biochemistry Survey Course.