Hydrophobic surfactant proteins induce a phosphatidylethanolamine to form cubic phases

Citations of this article
Mendeley users who have this article in their library.


The hydrophobic surfactant proteins SP-B and SP-C promote rapid adsorption of pulmonary surfactant to an air/ water interface. Previous evidence suggests that they achieve this effect by facilitating the formation of a rate-limiting negatively curved stalk between the vesicular bilayer and the interface. To determine whether the proteins can alter the curvature of lipid leaflets, we used x-ray diffraction to investigate how the physiological mixture of these proteins affects structures formed by 1-palmitoyl-2-oleoyl phosphatidylethanolamine, which by itself undergoes the lamellar-to-inverse hexagonal phase transition at 71°C. In amounts as low as 0.03% (w:w) and at temperatures as low as 57°C, the proteins induce formation of bicontinuous inverse cubic phases. The proteins produce a dose-related shift of diffracted intensity to the cubic phases, with minimal evidence of other structures above 0.1% and 62°C, but no change in the lattice-constants of the lamellar or cubic phases. The induction of the bicontinuous cubic phases, in which the individual lipid leaflets have the same saddle-shaped curvature as the hypothetical stalk-intermediate, supports the proposed model of how the surfactant proteins promote adsorption. © 2010 by the Biophysical Society.




Chavarha, M., Khoojlnlan, H., Schulwitz, L. E., Biswas, S. C., Rananavare, S. B., & Hall, S. B. (2010). Hydrophobic surfactant proteins induce a phosphatidylethanolamine to form cubic phases. Biophysical Journal, 98(8), 1549–1557. https://doi.org/10.1016/j.bpj.2009.12.4302

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free