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Science 23 July 1993:
Vol. 261. no. 5120, pp. 453 - 456
DOI: 10.1126/science.8332910
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Articles
Science, Vol 261, Issue 5120, 453-456
Copyright © 1993 by American Association for the Advancement of Science
A function of lung surfactant protein SP-B
ML Longo,
AM Bisagno,
JA Zasadzinski,
R Bruni,
and
AJ Waring
Department of Chemical and Nuclear Engineering, University of California, Santa Barbara 93106.
The primary function of lung surfactant is to form monolayers at the alveolar interface capable of lowering the normal surface tension to near zero. To accomplish this process, the surfactant must be capable of maintaining a coherent, tightly packed monolayer that avoids collapse during expiration. The positively charged amino-terminal peptide SP-B1-25 of lung surfactant-specific protein SP-B increases the collapse pressure of an important component of lung surfactant, palmitic acid (PA), to nearly 70 millinewtons per meter. This alteration of the PA isotherms removes the driving force for "squeeze-out" of the fatty acids from the primarily dipalmitoylphosphatidylcholine monolayers of lung surfactant. An uncharged mutant of SP-B1-25 induced little change in the isotherms, suggesting that a specific charge interaction between the cationic peptide and the anionic lipid is responsible for the stabilization. The effect of SP-B1-25 on fatty acid isotherms is remarkably similar to that of simple poly-cations, suggesting that such polymers might be useful as components of replacement surfactants for the treatment of respiratory distress syndrome.
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