Porcine pulmonary surfactant preparations contain the antibacterial peptide prophenin and a C-terminal 18-residue fragment thereof

详细信息    查看全文

• 作者：Wang ; Yuqin ; Griffiths ; William J. ; Curstedt ; Tore ; Johansson ; Jan
• 关键词：Pulmonary surfactant ; Lipid-associated peptide ; Peptide isolation ; Antibacterial peptide ; Cathelicidin ; Mass spectrometry ; CID ; collision induced dissociation ; ES ; electrospray ; HPLC ; high performance liquid chromatography ; LB ; Luria-Bertani ; MALDI-TOF ; m
• 刊名：FEBS Letters
• 出版年：1999
• 出版时间：October 29, 1999
• 年：1999
• 卷：460
• 期：2
• 页码：257-262
• 全文大小：82.3 K

文摘

Surfactant preparations obtained from porcine lungs by extraction with chloroform/methanol followed by chromatography over Lipidex-5000 are used for treatment of respiratory distress syndrome in preterm infants. These preparations contain about 98 % phospholipids and 1–2 % of the hydrophobic pulmonary surfactant-associated proteins B and C (SP-B and SP-C). Separation of the proteins in the surfactant preparation by reversed-phase high performance liquid chromatography revealed, in addition to SP-B and SP-C, the presence of three peptides derived from the cathelicidin family of antibacterial peptides. The 79-residue proline-rich peptide prophenin (identical to that isolated from leukocytes), an 80-residue prophenin with an N-terminal pyroglutamic acid residue, and a C-terminal 18-residue fragment of prophenin were found in approximate molar ratios of 1:20:5. A synthetic version of the C-terminal 18-residue peptide exhibits salt-dependent antibacterial activity (higher activity in the absence of salt) against the Gram-positive bacterium Bacillus megaterium Bm11 and, to a lesser extent, against Gram-negative Escherichia coli D21 cells. It appears possible that the presence of prophenin peptides may contribute to the antibacterial properties of surfactant preparations.