Antibodies against synthetic amphipathic helical sequences of surfactant protein SP-B detect a conformational change in the native protein.
Synthetic peptides based on the native human sequence of surfactant protein B have been used to generate polyclonal monospecific antibodies against specific segments of the native SP-B protein. Circular dichroism analysis of the synthetic peptides shows they have a dominant helical content in structure promoting environments and tensiometric measurements indicate these peptides lower surface tension at air-water interfaces implying that they contain amphipathic alpha helical motifs. Antibodies directed against the C-terminal segment of SP-B react with the native protein in the oxidized and reduced state. Antibodies directed against the N-terminal sequence of SP-B react with the native protein only in the reduced state suggesting that this domain has a conformation dependent on disulfide bond formation.
Fan
B R
BR
Department of Pediatrics, King/Drew Medical Center-UCLA 90059.
Bruni
R
R
Taeusch
H W
HW
Findlay
R
R
Waring
A J
AJ
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry / Q000276:immunology; D011487:Protein Conformation; D011510:Proteolipids / Q000276:immunology*; D011663:Pulmonary Surfactants / Q000276:immunology* / Q000648:ultrastructure; D013329:Structure-Activity Relationship; D013499:Surface Properties
D010455:Peptides; D011510:Proteolipids; D011663:Pulmonary Surfactants