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Updated: Aug 16, 2026

Real-time Monitoring of Ligand-receptor Interactions with Fluorescence Resonance Energy Transfer
Published on: August 20, 2012
A diether phosphonolipid surfactant analog, DEPN-8, is resistant to phospholipase-C cleavage
W H Lin1, S G Cramer, J G Turcotte
1Department of Chemistry, University of Connecticut, West Hartford, USA.
Abstract:
Increased activities of phospholipase A2 and C (PLC) have been observed in the bronchoalveolar lavages of patients with adult respiratory distress syndrome (ARDS). DL-alpha-Di-O-hexadecylphosphonocholine [(R)(S)-DEPN-8], a surfactant analog of superior surface activity to the major lung surfactant phospholipid, dipalmitoylphosphatidylcholine (DPPC), is not a substrate for phospholipases A1, A2 and D, but is a substrate for PLC. (R)(S)-DEPN-8 was found in vitro to undergo significantly less PLC-catalyzed degradation as compared to DPPC. The results suggest that (R)(S)-DEPN-8 and structurally related analogs may be useful as components of exogenous replacement surfactant formulations for the treatment of ARDS-related lung injuries.
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