Phospholipase-vesicle interaction

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Cao, Hsu, Y.H., Li, S., et al. (2011) Lipoprotein-associated phospholipase A interacts with phospholipid vesicles via a surface-disposed hydrophobic a-helix. Biochemistry, 50 (23), 5314-5321. 

IR spectroscopy of the X-receptor protein signal peptide in phospholipid monolayers shows that the peptide affects the packing of the lipid hydrocarbon tails (M. S. Briggs, R. A. Dluhy, D. G. Cornell, and L. M. Gierasch, unpublished results). In samples formed at the same surface pressure, the lipid tails are oriented differendy in the presence and absence of signal peptide. A phospholipase assay for structural defects in phospholipid bilayers (Jain et al., 1984) indicates that the X-receptor protein signal peptide interacts with vesicles to induce such defects. The peptides perturb the lipid structure at lower mole fractions than do various lysophospholipids. These data provide yet another indication that signal peptides interact with and perturb lipid complexes. 

Burke, IE., Karbarz, M.J.,Deems, R.A., Li, S.,Woods,V.L., Dennis, E.A. (2008) Interaction of group lA phospholipase A2 with metal ions and phospholipid vesicles probed with deuterium exchange mass spectrometry. Biochemistry, 47, 6451-6459. 

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