Changes in membrane elasticity caused by the hydrophobic surfactant proteins correlate poorly with adsorption of lipid vesicles

Author:

Loney Ryan W.1234,Brandner Bret1234ORCID,Dagan Maayan P.1234,Smith Paige N.1234ORCID,Roche Megan56784,Fritz Jonathan R.56784ORCID,Hall Stephen B.1234ORCID,Tristram-Nagle Stephanie A.56784ORCID

Affiliation:

1. Pulmonary and Critical Care Medicine

2. Oregon Health & Science University

3. Portland

4. USA

5. Biological Physics Group

6. Department of Physics

7. Carnegie Mellon University

8. Pittsburgh

Abstract

We used X-ray diffuse scattering to determine the bending modulus of lipid bilayers and an order parameter of the acyl chains to establish how the hydrophobic surfactant proteins, SP-B and SP-C, promote adsorption of lipids to an air/water interface.

Funder

National Heart, Lung, and Blood Institute

Publisher

Royal Society of Chemistry (RSC)

Subject

Condensed Matter Physics,General Chemistry

Reference75 articles.

1. J. Goerke and J. A.Clements , in Handbook of Physiology – The Respiratory System. Vol. III, Part 1 , ed. P. T. Macklem and J. Mead , American Physiological Society , Washington, D.C. , 1985 , vol. III, pp. 247–261

2. B. Robertson , in Pulmonary Surfactant , ed. B. Robertson , L. M. G. Van Golde and J. J. Batenburg , Elsevier Science Publishers , Amsterdam , 1st edn, 1984 , pp. 383–418

3. Alterations in SP-B and SP-C Expression in Neonatal Lung Disease

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