Journal of Undergraduate Research
Keywords
secretory phospholipase A2, sPLA2, binding properties, fluorescent probe nystatin
College
Life Sciences
Department
Physiology and Developmental Biology
Abstract
Nystatin is a fluorescent molecule that has recently been characterized as a probe of phospholipid properties in artificial membranes. The hypothesis purported by my research group was that nystatin binds preferentially to the boundary between ordered and disordered phases of phospholipids in both artificial and biological membranes. My project was to test this hypothesis in biological membranes. By further characterizing nystatin as a probe, our group would have another tool with which to understand the binding properties of the enzyme secretory phospholipase A2 (sPLA2). Secretory PLA2 adsorbs to the surface of cells and hydrolyzes membrane phospholipids to release free fatty acid. Normal healthy cells resist this digestive function, but in contrast, apoptotic cells are susceptible (Nielson, 2000). Secretory PLA2 binding is influenced by phospholipid properties. It has been concluded that sPLA2 prefers to hydrolyze lipids primarily at the boundaries between ordered and disordered domains (Best, K.B.). Thus, if the hypothesis were correct, nystatin would be a perfect probe to investigate the properties of membranes that are susceptible to sPLA2.
Recommended Citation
Bailey, Rachel Williams and Bell, Dr. John
(2013)
"Determining Secretory Phospholipase A2 Binding Properties Through the Fluorescent Probe Nystatin,"
Journal of Undergraduate Research: Vol. 2013:
Iss.
1, Article 1417.
Available at:
https://scholarsarchive.byu.edu/jur/vol2013/iss1/1417