Imaging of monolayers composed of palmitic acid and lung surfactant protein B.

摘要

Near-field scanning optical microscopy and atomic force microscopy are used to probe the sub-micrometre phase structure in palmitic acid monolayers containing the 25 peptide amino terminus of lung surfactant protein B (SP-B(1-25)). Monolayers deposited onto mica substrates at a surface pressure of 15 mN m-1 exhibit a two-phase coexistence across a broad range of SP-B(1-25) concentrations. Monolayers containing 5 wt.% SP-B(1-25) or less exhibit an expanse of liquid condensed phase in which elliptical liquid expanded (LE) domains with areas of approximately 25 microm2 coexist. By contrast, monolayers containing 20 wt.% SP-B(1-25) exhibit an expanse of liquid expanded phase in which circular liquid condensed domains coexist. The phase distribution dependence on SP-B(1-25) concentration suggests that the peptide induces disorder in the monolayer.