0000000000125600
AUTHOR
Olga L. Ospina
showing 2 related works from this author
Membrane-Perturbing Activities of KL4-Related Surfactant Peptides
2013
KL4 is a 21-residue peptide proposed as a potential substitute of pulmonary surfactant protein SP-B in synthetic surfactants, intended for the treatment of respiratory pathologies. The peptide, composed by leucines interrupted by lysine every four residues, was synthesized to simulate C-terminal amphipathic helical segments of SP-B. Once incorporated into lipid-protein complexes, KL4 promotes formation of interfacial films that produce and maintain surface tensions below 5 mN/m during compression-expansion cycling. Although KL4 was designed as an amphipathic helix at the membrane surface, the data on orientation and interactions of the peptide in membranes are contradictory. In the present …
Palmitoylation of Pulmonary Surfactant Protein SP-C Is Critical for Its Functional Cooperation with SP-B to Sustain Compression/Expansion Dynamics in…
2010
AbstractRecent data suggest that a functional cooperation between surfactant proteins SP-B and SP-C may be required to sustain a proper compression-expansion dynamics in the presence of physiological proportions of cholesterol. SP-C is a dually palmitoylated polypeptide of 4.2 kDa, but the role of acylation in SP-C activity is not completely understood. In this work we have compared the behavior of native palmitoylated SP-C and recombinant nonpalmitoylated versions of SP-C produced in bacteria to get a detailed insight into the importance of the palmitic chains to optimize interfacial performance of cholesterol-containing surfactant films. We found that palmitoylation of SP-C is not essenti…