| Autor: |
Johansson J; Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden., Gustafsson M, Palmblad M, Zaltash S, Robertson B, Curstedt T |
| Jazyk: |
angličtina |
| Zdroj: |
Biology of the neonate [Biol Neonate] 1998 Sep; Vol. 74 Suppl 1, pp. 9-14. |
| DOI: |
10.1159/000047029 |
| Abstrakt: |
Surfactant preparations for the treatment of respiratory distress syndrome (RDS) that contain phospholipids and small amounts of the two hydrophobic proteins, SP-B and SP-C, are presently obtained from animal lungs. Since structural information about SP-B and SP-C is available, it appears possible to design analogues that can replace the native proteins in synthetic surfactants. SP-C contains a single helix, but analogues with the poly-Val sequence of the native molecule do not fold into a native-like alpha-helical conformation. However, replacement of all Val with Leu yields efficient folding into a helical structure and Leu-based SP-C analogues effectively accelerate spreading of surfactant lipids and exhibit some physiological activity in animal models of RDS. The inferior in vivo activity of synthetic surfactants containing SP-C only compared to that of surfactant preparations derived from natural sources may be caused by a lack of covalently linked palmitoyl groups in the analogues and/or absence of SP-B. SP-B is significantly larger than SP-C and has a tertiary fold of several amphipathic helices in a dimeric structure. A single simplified amphipathic helical peptide containing only Leu and Lys does not mimic the surface properties of SP-B in vitro. These circumstances make the design of SP-B analogues from solely structural considerations less likely to be successful than in the case of SP-C. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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