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Science 25 October 1991:
Vol. 254. no. 5031, pp. 566 - 568
DOI: 10.1126/science.1948032
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Articles

Science, Vol 254, Issue 5031, 566-568
Copyright © 1991 by American Association for the Advancement of Science

articles

Pulmonary surfactant protein B (SP-B): structure-function relationships

CG Cochrane and SD Revak

Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.

SP-B is a protein in pulmonary surfactant that is, in greatest part, responsible for resistance to surface tension and prevention of collapse of pulmonary alveoli. Peptides of 21 residues, synthesized following the sequence of SP-B or resembling the hydrophobic and hydrophilic domains of SP-B (such as RLLLLRLLLLRLLLLRLLLLR, R, Arg, and L, Leu), enhanced the abilities of phospholipids to reduce surface tension both in vitro and in vivo. Intermittent positively charged residues were essential for this activity. The SP-B-like peptides were found by tryptophan fluorescence to partition within the phospholipid layer in contact with both polar head groups and acyl side chains. These data, together with findings that the SP-B-related peptides increase inter- and intramolecular order of the phospholipid layer, suggest that SP-B resists surface tension by increasing lateral stability of the phospholipid layer.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)