The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B
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- The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B
- Joo Hyun Kang; Myung Kyu Lee; Kil Lyong Kim; Kyung Soo Hahm
- Bibliographic Citation
- Biochemistry and Molecular Biology International, vol. 40, no. 3, pp. 617-627
- Publication Year
- Synthetic pulmonary surfactants consisting of a mixture of phospholipids with synthetic peptides based on human and bovine surfactant-associated protein SP-B were prepared. These surfactants were analyzed for their biophysical activities by Wilhemly balance experiments and for their secondary structures by circular dichroism (CD) spectroscopy. Four synthetic peptides (SP-1, SP-2, SP-3, and SP-4) combined with the phospholipid mixture displayed significant surfactant properties. The CD spectra showed that the α-helical propensities of the peptides in SDS micelles were related to their surfactant activities. These results suggested that the several truncated peptides originated from SP-B protein, when appropriately recombined with phospholipids, could be used as an effective synthetic surfactant for clinical use.
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