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Biophysical Journal 85:2397-2405 (2003)
© 2003 The Biophysical Society

Interaction of Pulmonary Surfactant Protein SP-A with DPPC/Egg-PG Bilayers

Michael R. Morrow *, Nidal Abu-Libdeh *, June Stewart {dagger} and Kevin M. W. Keough {dagger} {ddagger}

* Department of Physics and Physical Oceanography, {dagger} Department of Biochemistry, and {ddagger} Discipline of Pediatrics, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X9 Canada

Correspondence: Address reprint requests to Dr. Kevin Keough, Dept. of Biochemistry, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X9, Canada. Tel.: 709-737-2530; Fax: 709-737-2552; E-mail: kkeough@mun.ca or Dr. Michael Morrow, Dept. of Physics and Physical Oceanography, Memorial University of Newfoundland, St. John's, Newfoundland, A1B 3X7, Canada. Tel.: 709-737-4361; Fax: 709-737-8739; E-mail: myke@physics.mun.ca.

In the mixture of lipids and proteins which comprise pulmonary surfactant, the dominant protein by mass is surfactant protein A (SP-A), a hydrophilic glycoprotein. SP-A forms octadecamers that interact with phospholipid bilayer surfaces in the presence of calcium. Deuterium NMR was used to characterize the perturbation by SP-A, in the presence of 5 mM Ca2+, of dipalmitoyl phosphatidylcholine (DPPC) properties in DPPC/egg-PG (7:3) bilayers. Effects of SP-A were uniformly distributed over the observed DPPC population. SP-A reduced DPPC chain orientational order significantly in the gel phase but only slightly in the liquid-crystalline phase. Quadrupole echo decay times for DPPC chain deuterons were sensitive to SP-A in the liquid-crystalline mixture but not in the gel phase. SP-A reduced quadrupole splittings of DPPC choline ß-deuterons but had little effect on choline {alpha}-deuteron splittings. The observed effects of SP-A on DPPC/egg-PG bilayer properties differ from those of the hydrophobic surfactant proteins SP-B and SP-C. This is consistent with the expectation that SP-A interacts primarily at bilayer surfaces.




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