Interference by bovine serum albumin in PED6 based phospholipase A2 screening assays

Authors: Pohjala, L. L.; Sairio, N. K.; Vuorela, P. M.

Source: Die Pharmazie - An International Journal of Pharmaceutical Sciences, Volume 67, Number 11, November 2012 , pp. 954-955(2)

Publisher: Govi-Verlag

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Phospholipase A2 (PLA2) enzymes are emerging drug targets in anti-inflammatory therapy and various assay formats are available for hit discovery on these enzymes. In several assay protocols for measuring PLA2 activity, bovine serum albumin (BSA) is used to improve the signal linearity. Here, we show that BSA is able to convert PED6, a profluorescent phosphatidylethanolamine analogue commonly used as a PLA2 substrate probe, to a fluorescent form in a similar fashion as PLA2. The reaction is concentration-dependent, occurs more efficiently in phosphotidylglycerol than phosphatidylcholine vesicles and is sensitive to a PLA2 inhibitor aristolochic acid. These results indicate that BSA may represent a source of assay interference when screening against PLA2 enzymes and it should not be applied with PED6.

Document Type: Short Communication


Publication date: November 1, 2012

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  • Pharmazie is one of the world's leading pharmaceutical journals. As a peer-reviewed scientific journal, DiePharmazie is regularly indexed in Current Contents/Life Sciences, Excerpta Medica, Analytical Abstracts, International Pharmaceutical Abstracts, Beilstein Current Facts in Chemistry, Chemical Engineering and Biotechnology Abstracts (CEABA) and Science Citation Index.
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