Abstract
This letter describes a new method for studying the interaction of the membrane-lysing enzyme phospholipase A(2) (PLA(2)) with phospholipid bilayers by simultaneous measurements of enzyme binding and vesicle lysis using surface plasmon resonance (SPR) and permeabilization using surface plasmon field-enhanced fluorescence spectroscopy (SPFS). The PLA(2) inhibitor dimethyl-eicosadienoic acid was incorporated into the surface-bound vesicles and support bilayer in order to study its role in preventing PLA(2)-mediated vesicle lysis. This methodology has a generic applicability for the study of a range of membrane-disrupting agents.
Original language | English |
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Pages (from-to) | 6473-6476 |
Number of pages | 4 |
Journal | Langmuir |
Volume | 22 |
Issue number | 15 |
DOIs | |
Publication status | Published - 2006 |