Surface Dilatational Behavior of Pulmonary Surfactant Components Spread on the Surface of a Captive Bubble. 3. Dipalmitoyl Phosphatidylcholine, Surfactant Protein C, and Surfactant Protein B

Langmuir ◽  
2003 ◽  
Vol 19 (18) ◽  
pp. 7521-7527 ◽  
Author(s):  
N. Wüstneck ◽  
R. Wüstneck ◽  
U. Pison
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Dipalmitoyl Phosphatidylcholine ◽  
Surfactant Protein C ◽  
Surfactant Protein B ◽  
Protein B

Effect of Dexamethasone on Gene Expression of Surfactant Protein B and Surfactant Protein C

2003 ◽  
Vol 54 (4) ◽  
pp. 439
Author(s):  
Ik Soo Park ◽  
Jang Won Sohn ◽  
Ho Joo Yoon ◽  
Dong Ho Shin ◽  
Sung Soo Park
Keyword(s):  
Gene Expression ◽  
Protein C ◽  
Surfactant Protein ◽  
Surfactant Protein C ◽  
Surfactant Protein B ◽  
Protein B

scholarly journals Amyloid fibril formation by pulmonary surfactant protein C

FEBS Letters ◽  
1999 ◽  
Vol 464 (3) ◽  
pp. 138-142 ◽  
Author(s):  
Magnus Gustafsson ◽  
Johan Thyberg ◽  
Jan Näslund ◽  
Erik Eliasson ◽  
Jan Johansson
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Amyloid Fibril ◽  
Surfactant Protein ◽  
Fibril Formation ◽  
Surfactant Protein C ◽  
Amyloid Fibril Formation ◽  
Pulmonary Surfactant Protein

scholarly journals A method for S- and O-palmitoylation of peptides: synthesis of pulmonary surfactant protein-C models

1999 ◽  
Vol 343 (3) ◽  
pp. 557-562 ◽  
Author(s):  
Esmail YOUSEFI-SALAKDEH ◽  
Jan JOHANSSON ◽  
Roger STRÖMBERG
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Cd Spectroscopy ◽  
Reversed Phase ◽  
Prolonged Treatment ◽  
Surfactant Protein C ◽  
Palmitoyl Chloride ◽  
Α Helix ◽  
Pulmonary Surfactant Protein

A method for O- and S-palmitoylation of non-protected peptides has been developed. The peptides are treated with excess of palmitoyl chloride in 100% trifluoroacetic acid for 10 min at room temperature. The acidic conditions prevent acylation of amino groups, which is only significant after prolonged treatment (hours to days). The tripeptides Gly-Cys-Phe and Gly-Ser-Phe were converted into the respective S- and O-palmitoylated compounds, and the hydrophobic pulmonary surfactant protein-C model peptides, LRIPCCPVNLKRLLVVV [SP-C(1-17)] and FGIPSSPVLKRLLILLLLLLLILLLILGALLMGL [SP-C(Leu)] were converted into their respective S,S- and O,O-dipalmitoylated peptides. The reactions were virtually quantitative, and the palmitoylated peptides were isolated in about 75-80% yield after reversed-phase HPLC purification. CD spectroscopy showed that S,S-dipalmitoylation of SP-C(1-17) affects the peptide secondary structure (substantial increase in the α-helix content) in dodecylphosphocholine micelles.

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