Examination of the peptide sequence requirements for lipid-binding. Alternative pathways for promoting the interaction of amphipathic alpha-helical peptides with phosphatidylcholine.

  title={Examination of the peptide sequence requirements for lipid-binding. Alternative pathways for promoting the interaction of amphipathic alpha-helical peptides with phosphatidylcholine.},
  author={Larry R. McLean and Karen A. Hagaman and Thomas J. Owen and Marguerite H. Payne and W. Sean Davidson and John L Krstenansky},
  journal={Biochimica et biophysica acta},
  volume={1086 1},
Study of tensioactive properties of casein signal peptides and their interactions with phospholipids.
The physico-chemical measures of interactions of signal peptides of casein beta and alpha s2 confirm their mutual genetic relationship, and on the other hand they show the divergence of case in beta andalpha s2 from casein kappa signal peptide.
Effect of membrane-partitioned n-alcohols and fatty acids on pore-forming activity of a sea anemone toxin
Abstract Equinatoxin II, a 19.8 kDa pore-forming toxin from the sea anemone Actinia equina, was examined for hemolytic activity and permeabilization of small unilamellar lipid vesicles (SUV) in the
Biophysical characterization of interaction between apolipoprotein A-I and bacterial lipopolysaccharide
The changes found in the micellization process are likely to be mainly caused by changes in the apo A-I conformation by LPS interaction in solution.
Spectroscopic and functional characterization of the putative transmembrane segment of the minK potassium channel.
A role of the transmembrane segment of minK both in the assembly and as a constituent of the pore formed by the protein is experimentally supported.
High yield overexpression and characterization of human recombinant proapolipoprotein A-I.
It is concluded that proapoA-I expressed and purified from E. coli is functionally and structurally indistinguishable from mature apoA- I purified from plasma when analyzed in vitro.
Biomimetic pulmonary surfactants.


Minimal peptide length for interaction of amphipathic alpha-helical peptides with phosphatidylcholine liposomes.
The interactions of a series of amphipathic alpha-helical peptides containing from 6 to 18 amino acid residues with dipalmitoylphosphatidylcholine and DPPC were studied by optical and calorimetric methods and formed small micellar structures, as judged by gel filtration chromatography.
Effect of micelle diameter on tryptophan dynamics in an amphipathic helical peptide in phosphatidylcholine.
The effect of dimyristoylphosphatidylcholine (DMPC) on the conformation and environment of the single tryptophan residue of a model amphipathic helical polypeptide has been investigated by
Presence of an amphipathic helical segment and its relationship to biological potency of calcitonin analogs.
The ability of a calcitonin analog to form structures of higher helical content in the presence of amphiphiles is a requirement for the analog to exhibit high potency in assays of biological activity.
Lipid-protein interactions in the plasma lipoproteins.
A rapid method for the synthesis of protein-lipid complexes using adsorption chromatography.
Results are described which show the application of this method to the study of lipid variation on the structure of model HDL, including the alteration of lipid-protein molar ratios and the addition of cholesterol.