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Biophys J, March 1998, p. 1101-1109, Vol. 74, No. 3
*Departmento de Bioquímica, Facultad de Biología,
Universidad Complutense, 28040 Madrid, Spain, and the
Department of Biochemistry and
Discipline
of Pediatrics, Memorial University of Newfoundland, St. John's,
Newfoundland A1B 3X9, Canada
The interaction of the pulmonary surfactant protein SP-A
fluorescently labeled with Texas Red (TR-SP-A) with monolayers of dipalmitoylphosphatidylcholine (DPPC) and
DPPC/dipalmitoylphosphatidylglycerol 7:3 w/w has been investigated. The
monolayers were spread on aqueous subphases containing TR-SP-A. TR-SP-A
interacted with the monolayers of DPPC to accumulate at the boundary
regions between liquid condensed (LC) and liquid expanded (LE) phases.
Some TR-SP-A appeared in the LE phase but not in the LC phase. At
intermediate surface pressures (10-20 mN/m), the protein caused the
occurrence of more, smaller condensed domains, and it appeared to be
excluded from the monolayers at surface pressure in the range of 30-40
mN/m. TR-SP-A interaction with DPPC/dipalmitoylphosphatidylglycerol monolayers was different. The protein did not appear in either LE or LC
but only in large aggregates at the LC-LE boundary regions, a
distribution visually similar to that of fluorescently labeled concanavalin A adsorbed onto monolayers of DPPC. The observations are
consistent with a selectivity of interaction of SP-A with DPPC and for
its accumulation in boundaries between LC and LE phase.
Biophys J, March 1998, p. 1101-1109, Vol. 74, No. 3
© 1998 by the Biophysical Society 0006-3495/98/03/1101/09 $2.00
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