R Suzanne Farver

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Bis(monoacylglycero)phosphate (BMP) is an endosomal lipid with a unique structure that is implicated in the formation of intraendosomal vesicular bodies. Here we have characterized the effects of dioleoyl-BMP (BMP(18:1)) at concentrations of 5, 10, 15 and 20mol% on the thermotropic behavior of dipalmitoyl phosphatidylcholine (DPPC) vesicles, and compared(More)
Pulmonary surfactant protein B (SP-B) is an essential protein for lowering surface tension in the alveoli. SP-B(1-25), a peptide comprised of the N-terminal 25 amino-acid residues of SP-B, is known to retain much of the biological activity of SP-B. Circular dichroism has shown that when SP-B(1-25) interacts with negatively charged lipid vesicles, it(More)
KL(4) is a 21-residue functional peptide mimic of lung surfactant protein B, an essential protein for lowering surface tension in the alveoli. Its ability to modify lipid properties and restore lung compliance was investigated with circular dichroism, differential scanning calorimetry, and solid-state NMR spectroscopy. KL(4) binds fluid lamellar phase PC/PG(More)
Lung surfactant protein B (SP-B) is a lipophilic protein critical to lung function at ambient pressure. KL(4) is a 21-residue peptide which has successfully replaced SP-B in clinical trials of synthetic lung surfactants. CD and FTIR measurements indicate KL(4) is helical in a lipid bilayer environment, but its exact secondary structure and orientation(More)
Lung surfactant protein B (SP-B) is critical to minimizing surface tension in the alveoli. The C-terminus of SP-B, residues 59-80, has much of the surface activity of the full protein and serves as a template for the development of synthetic surfactant replacements. The molecular mechanisms responsible for its ability to restore lung compliance were(More)
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