Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids.
Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids.
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肺表面活性剂 SP-C 二级结构和取向的傅里叶变换红外研究及其对磷脂动态表面性质的影响。
DOI:
10.1021/bi00105a033
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发表时间:
1991
期刊:
影响因子:
2.9
通讯作者:
Mendelsohn,R
中科院分区:
文献类型:
--
作者:
Pastrana,B;Mautone,AJ;Mendelsohn,R
Department of Chemistry, Newark College of Arts and Sciences, Rutgers University, 73 Warren Street, Newark, New Jersey 07102, and Departments of Anesthesiology and Physiology, University of Medicine and Dentistry of New Jersey—New Jersey Medical School, 185 South Orange Avenue, Newark, New Jersey 07102 Received June 4, 1991; Revised Manuscript Received August 7, 1991 abstract: SP-C, a highly hydrophobic, 3.7-kDa protein constituent of lung surfactant, has been isolated from bovine lung lavage, purified, and reconstituted into binary lipid mixtures of 1, 2-dipalmitoyl-phosphatidylcholine (DPPC) and 1, 2-dipalmitoylphosphatidylglycerol (DPPG). Fourier transform infrared (FT-IR) spectroscopy has been applied to examine SP-C secondary structure, the average orientation of-helical segments relative to the bilayer normal in membrane films, and the effect of protein on the thermotropic properties of the phospholipid acylchains. In addition, dynamic surface measurements were made on phospholipid films at the A/W interface in the presence and absence of SP-C. SP-C (0.5 mol%) was found to possess about 60%-helical secondary structure in lipid vesicles. Higher levels (1.5 mol%) of SP-C resulted in a slight increase of/?-forms, possiblyresulting from protein aggregation. The helical segments exhibited an average angle of orientation of about 24 with respect to thebilayer normal, suggesting a trans-bilayer orientation of the peptide. The observation that 70% of the peptide bond hydrogens are hard to exchange in D20 further reflectsthe hydrophobic nature of the molecule. SP-C produced little effect on the thermotropic properties of the binary lipid mixture, as measured from acyl chain CH and CD stretching frequencies. However, thepresence of 1 mol% protein markedly reduced the viscance and increased the elasticity of surface films, suggesting a mechanism by which SP-C facilitates the spreading of phospholipids on an aqueous surface. The possible physiological consequences of these observations are discussed.I^ lmonary surfactant, a mixture of lipids and proteins se-creted by type II pneumocytes, possesses as its essential physical characteristic the ability to lower surface tension at the air/alveolar interface to near zero (Scarpelli, 1988). The main lipid in surfactant is 1, 2-dipalmitoylphosphatidylcholine (DPPC), 1 with smalleramounts of phosphatidylglycerol (PG), unsaturated PCs, other anionic phospholipids, and cholesterol. Several surfactant protein classes have been identified. The most abundant is a family (termed SP-A) with a molecular weight range of 28-36K. Ng et al.(1983) have shown this class to be subject to variable posttranslational glycosylation. The gene for human pulmonary SP-A has been isolated and characterized (White et al., 1985). In addition to SP-A, two smaller hydrophobic proteins are also present, namely, SP-B, a 79 amino acid fragment that is the processing product of residues 201-279 from a 42-kDa precursor (Curstedt et al., 1988), and SP-C, a highly hydrophobic moiety (Johansson et al., 1988; Hawgood et al., 1987). The N-terminus of SP-C is heterogeneous, the main form being 35 residueslong (Jo-hansson et al., 1988), with S-palmitoylated cysteine residues present in the porcine species (Curstedt et al., 1990). Recently, Persson et al.(1990) have reported the isolation of a col-lagenous surfactant-associated glycoprotein, SP-D. The functions of the various protein classes have generally been assumed to be related to surfactant adsorption and spreading at the A/W interface and its reuptake into type II
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DOI:
10.1016/0005-2760(83)90164-9
发表时间:
1983
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Ng,VL;Herndon,VL;Mendelson,CR;Snyder,JM
通讯作者:
Snyder,JM
影响因子:
2.9
作者:
J. Johansson;T. Curstedt;B. Robertson;H. Jörnvall
通讯作者:
H. Jörnvall
影响因子:
64.8
作者:
R. T. White;D. Damm;Judy Miller;K. Spratt;J. Schilling;S. Hawgood;B. Benson;B. Cordell
通讯作者:
R. T. White;D. Damm;Judy Miller;K. Spratt;J. Schilling;S. Hawgood;B. Benson;B. Cordell
影响因子:
3.4
作者:
K. Rothschild;N. Clark
通讯作者:
N. Clark
DOI:
10.1016/0005-2736(87)90349-x
发表时间:
1987
期刊:
Biochimica et biophysica acta
影响因子:
--
作者:
Mautone,AJ;Reilly,KE;Mendelsohn,R
通讯作者:
Mendelsohn,R