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Structural and Functional Importance of the C‐Terminal Part of the Pulmonary Surfactant Polypeptide SP‐C

par Clercx, Anne ;Vandenbussche, Guy ;Curstedt, Tore;Johansson, J;Jörnvall, H.;Ruysschaert, Jean Marie
Référence European journal of biochemistry / FEBS, 229, 2, page (465-472)
Publication Publié, 1995

Article révisé par les pairs

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Résumé :

A synthetic non‐palmitoylated form of the pulmonary surfactant protein SP‐C and three peptides of different lengths corresponding to its N‐terminal and middle parts were reconstituted into dipalmitoylglyc‐erophosphocholine/phosphatidylglycerol (7:3, by mass) lipid bilayers. The adsorption properties of each reconstituted system were determined by measurement of the surface pressure after injection of the samples underneath an air/water interface. Attenuated total reflection infrared spectroscopy provided information about the structure and orientation of peptides in lipid bilayers. The hydrophobic C‐terminal helix is crucial for the rapid adsorption as shortening of the C‐terminal part drastically restricted this activity. The C‐terminal amino acid sequence can however be replaced with that of the second transmembrane helix of bacteriorhodopsin without significantly modifying the adsorption properties. The data suggest that the hydrophobic C‐terminal part allows the anchorage of SP‐C in the lipid bilayer in such a manner that the N‐terminal domain adopts an optimal conformation and orientation for the rapid adsorption of phospholipids at the air/water interface, and/or that a membrane‐spanning helix as such is needed for this activity. Copyright © 1995, Wiley Blackwell. All rights reserved