This research studies the biophysical surface activity of synthetic phospholipids combined in vitro with purified lung surfactant apoprotein, having an M r of 6000. Hydrophobic surfactant.associated protein (SAP-6) was delipidated and purified from both bovine and canine lung lavage, and was combine
Hydrophobic homopolymeric peptides enhance the biophysical activity of synthetic lung phospholipids
โ Scribed by A.R. Venkitaraman; S.B. Hall; R.H. Notter
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 607 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0009-3084
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โฆ Synopsis
The effects of homopolymeric amino acids (molecular weight 2300 to 14,000) on the surface activity of dipalmitoyl phosphatidylcholine (DPPC) and DPPC/egg-phosphatidylglycerol (PG) were characterized by adsorption and dynamic surface tension lowering measurements at 37ยฐC. Homopolyamino acids studied included poly-L-leucine (poly-Leu) and poly-L-valine (poly-Val), since Leu and Val are known to be prominent in the structure of hydrophobic lung surfactant ~poprotein SP-B and SP-C. In addition, several other homopolyamino acids with varying hydrophobicity index were also iayestigated, including poly-L-phenylalanine (poly-Phe), poly-L-serine (poly-Ser), poly-L-lysine (poly-Lys) and poly-L-glutamic acigl (poly-Glu). Results showed that hydrophobic poly-Leu and poly-Phe at 1 and 10 weight percent greatly increased the adsorption facility of DPPC and DPPC/PG mixtures, with maximum surface pressures (up to 49 raN/m) near the equilibrium limit for phospholipid systems. In oscillating bubble studies, 1% mixture of poly-Leu or poly-Phe with DPPC or 8:2 DPPC/PG lowered surface tension into the range (near 1 mN/m) associated with active lung surfactant. In contrast, mixtures of DPPC and DPPC/PG with the more hydrophilic peptides poly-Ser, poly-Lys and poly-Glu showed little or no enhancement of surface activity over the phospholipids alone. Mixtures of poly-Val and phospholipids did not combine well with the simple co-sonication procedure used, and also exhibited little improvement in surface activity. Taken together, these results suggest that hydrophobicity is an important determinant for interactions of proteins with lung surfactant phospholipids, and that significant biophysical activity effects are not limited to highly specific amino acid sequences of the surfactant apoproteins, SP-B and SP-C. Simple homoamino acid polymers may provide useful model systems for investigating the specificity and character of some of these interactions, as well as the effectiveness of protein-phospholipid combination in synthetic surfactant mixtures.
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