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The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP‐B
Author(s) -
Kang Joo Hyun,
Lee Myung Kyu,
Kim Kil Lyong,
Hahm KyungSoo
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201213
Subject(s) - pulmonary surfactant , circular dichroism , phospholipid , chemistry , peptide , micelle , protein secondary structure , biochemistry , organic chemistry , aqueous solution , membrane
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.