Dimeric N-Terminal Segment of Human Surfactant Protein B (dSP-B 1–25) Has Enhanced Surface Properties Compared to Monomeric SP-B 1–25

Abstract

Surfactant protein B (SP-B) is a 17-kDa dimeric protein produced by alveolar type II cells. Its main function is to lower the surface tension by inserting lipids into the air/liquid interface of the lung. SP-B's function can be mimicked by a 25-amino acid peptide, SP-B 1–25, which is based on the N-terminal sequence of SP-B. We synthesized a dimeric version of this peptide, dSP-B 1–25, and the two peptides were tested for their surface activity. Both SP-B 1–25 and dSP-B 1–25 showed good lipid mixing and adsorption activities. The dimeric peptide showed activity comparable to that of native SP-B in the pressure-driven captive bubble surfactometer. Spread surface films led to stable near-zero minimum surface tensions during cycling while protein free, and films containing SP-B 1–25 lost material from the interface during compression. We propose that dimerization of the peptide is required to create a lipid reservoir attached to the monolayer from which new material can enter the surface film upon expansion of the air/liquid interface. The dimeric state of SP-B can fulfill the same function in vivo.