Abstract
In the current work we study with monolayer tensiometry and Brewster angle microscopy (BAM) the surface properties of Dipalmitoleoylphosphatidylethanolamine (DPoPE) films at the air/water interface in presence and absence of specific surfactant protein C (SP-C). DPoPE is used, as it readily forms both lamellar (Lα) and non-lamellar inverted hexagonal (HII) phases and appears as a suitable model phospholipid for probing the interfacial properties of distinct lipid phases. At pure air/water interface Lα shows faster adsorption and better surface disintegration than HII phase. The interaction of DPoPE molecules with SP-C (predeposited at the interface) results in equalizing of the interfacial disintegration of the both phases (reaching approximately the same equilibrium surface tension) although the adsorption kinetics of the lamellar phase remains much faster. Monolayer compression/decompression cycling revealed that the effect of SP-C on dynamic surface tensions (γ max and γ min) of mixed films is remarkably different for the two phases. If γ max for Lα decreased from the first to the third cycle, the opposite effect is registered for HII where γ max increases during cycling. Also the significant decrease of γ min for Lα in SP-C presence is not observed for HII phase. BAM studies reveal the formation of more uniform and homogeneously packed DPoPE monolayers in the presence of SP-C.
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Acknowledgments
This research was supported by The Scientific Foundation of Bulgarian Ministry of Education and Science (grant N BU-B-2/05). We also gratefully acknowledge the support of Prof. Boris Tenchov (Northwestern University, Department of Biochemistry, Molecular Biology and Cell Biology, Evanston, Illinois 60208) who supplied us with DPoPE and characterized the thermal bulk phase transitions of the phospholipid as described in our previous study (Jordanova et al. 2003).
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Jordanova, A., Georgiev, G.A., Alexandrov, S. et al. Influence of surfactant protein C on the interfacial behavior of phosphatidylethanolamine monolayers. Eur Biophys J 38, 369–379 (2009). https://doi.org/10.1007/s00249-008-0380-2
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DOI: https://doi.org/10.1007/s00249-008-0380-2