The relationships between biophysical activity and the secondary structure of synthetic peptides from the pulmonary surfactant protein SP-B.
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 alpha-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.
Peptide Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, KIST, Taejon, Korea.
J H
JH
Kang
M K
MK
Lee
K L
KL
Kim
K S
KS
Hahm
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D010743:Phospholipids / Q000737:chemistry; D017433:Protein Structure, Secondary; D011510:Proteolipids / Q000737:chemistry*; D011663:Pulmonary Surfactants / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013500:Surface Tension
D010446:Peptide Fragments; D010743:Phospholipids; D011510:Proteolipids; D011663:Pulmonary Surfactants