Imaging of monolayers composed of palmitic acid and lung surfactant protein B
| Autor: | Robert C. Dunn, Bret N. Flanders, Sarah A. Vickery |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
chemistry.chemical_classification
Microscopy Histology Chromatography Proteolipids Molecular Sequence Data Palmitic Acid Pulmonary Surfactants Peptide Microscopy Atomic Force Surface pressure Pathology and Forensic Medicine law.invention Palmitic acid Crystallography chemistry.chemical_compound chemistry Optical microscope Pulmonary surfactant law Phase (matter) Monolayer Amino Acid Sequence Mica |
| Zdroj: | Journal of Microscopy. 202:379-385 |
| ISSN: | 1365-2818 0022-2720 |
| DOI: | 10.1046/j.1365-2818.2001.00856.x |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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