The use of synthetic peptides in the formation of biophysically and biologically active pulmonary surfactants

• Published in: Pediatric research Vol. 29; no. 5; pp. 460 - 465
• Main Authors: Revak, S D, Merritt, T A, Hallman, M, Heldt, G, La Polla, R J, Hoey, K, Houghten, R A, Cochrane, C G
• Format: Journal Article
• Language: English
• Published: United States 01.05.1991
• Subjects: 1,2-Dipalmitoylphosphatidylcholine; Amino Acid Sequence; Animals; Apoproteins - chemical synthesis; Apoproteins - pharmacology; Lung - drug effects; Lung - embryology; Lung Compliance - drug effects; Molecular Sequence Data; Peptide Fragments - chemical synthesis; Peptide Fragments - pharmacology; Phosphatidylglycerols; Pulmonary Surfactant-Associated Proteins; Pulmonary Surfactants - chemical synthesis; Pulmonary Surfactants - pharmacology; Rabbits - embryology; Surface Tension
• ISSN: 0031-3998; 1530-0447
• DOI: 10.1203/00006450-199105010-00010

Synthetic pulmonary surfactants consisting of mixtures of phospholipids with synthetic peptides based on the amino acid sequence of human surfactant apoprotein SP-B were prepared. These surfactants were analyzed for their ability to lower surface tension on a pulsating bubble surfactometer and for their capacity to improve lung compliance and increase alveolar expansion in a fetal rabbit model of surfactant deficiency. The data demonstrate that several peptides, ranging from 17 to 45 residues in length, matching the carboxy-terminal sequence of the SP-B protein, when appropriately recombined with the phospholipid dipalmitoylphosphatidylcholine and phosphatidylglycerol (3:1), are capable of producing a synthetic surfactant with biophysical and biologic activity approaching that of human surfactant derived from amniotic fluid.