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

FEBS Letters

Curstedt, Tore²  Griffiths, William J¹  Johansson, Jan¹  Wang, Yuqin¹ 

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden;Department of Clinical Chemistry, Karolinska Institutet at Karolinska Hospital, S-171 76 Stockholm, Sweden

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;    matrix-assisted laser desorption/ionization time-of-flight;    OATOF;    orthogonal acceleration time-of-flight;    OATOFFPD;    orthogonal acceleration time-of-flight focal plane detector;    RDS;    respiratory distress syndrome;    RP;    reversed phase;    SP;    surfactant protein;    TFA;    trifluoroacetic acid;   

DOI  :  10.1016/S0014-5793(99)01363-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown