Dimeric N-terminal segment of human surfactant protein B (dSP-B(1-25)) has enhanced surface properties compared to monomeric SP-B(1-25).
Dimeric N-terminal segment of human surfactant protein B (dSP-B(1-25)) has enhanced surface properties compared to monomeric SP-B(1-25).
复制标题
与单体 SP-B(1-25) 相比,人表面活性剂蛋白 B (dSP-B(1-25)) 的二聚体 N 末端片段具有增强的表面特性。
DOI:
10.1016/s0006-3495(00)76299-0
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发表时间:
2000
期刊:
影响因子:
--
通讯作者:
Haagsman,HP
中科院分区:
文献类型:
--
作者:
Veldhuizen,EJ;Waring,AJ;Walther,FJ;Batenburg,JJ;vanGolde,LM;Haagsman,HP
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-B1–25, which is based on the N-terminal sequence of SP-B. We synthesized a dimeric version of this peptide, dSP-B1–25, and the two peptides were tested for their surface activity. Both SP-B1–25and dSP-B1–25showed 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-B1–25lost 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.