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

[1]  L. McLean,et al.  Minimal peptide length for interaction of amphipathic alpha-helical peptides with phosphatidylcholine liposomes. , 1991, Biochemistry.

[2]  L. McLean,et al.  Effect of micelle diameter on tryptophan dynamics in an amphipathic helical peptide in phosphatidylcholine. , 1989, Biochemistry.

[3]  H. Mantsch,et al.  Properties of lipid complexes with amphipathic helix-forming peptides. Role of distribution of peptide charges. , 1989, The Journal of biological chemistry.

[4]  L. McLean,et al.  Short model peptides having a high α‐helical tendency: Design and solution properties , 1989 .

[5]  L. McLean,et al.  Probucol reduces the rate of association of apolipoprotein C-III with dimyristoylphosphatidylcholine. , 1988, Biochimica et biophysica acta.

[6]  J. Swaney,et al.  A rapid method for the synthesis of protein-lipid complexes using adsorption chromatography. , 1988, Journal of lipid research.

[7]  G M Anantharamaiah,et al.  Studies of synthetic peptide analogs of the amphipathic helix. Effect of charge distribution, hydrophobicity, and secondary structure on lipid association and lecithin:cholesterol acyltransferase activation. , 1987, The Journal of biological chemistry.

[8]  G. Fourche,et al.  Morphological changes of phosphatidylcholine bilayers induced by melittin: vesicularization, fusion, discoidal particles. , 1986, Biochimica et biophysica acta.

[9]  J. C. Osborne,et al.  [21] Solution properties of apolipoproteins , 1986 .

[10]  R. Epand,et al.  Presence of an amphipathic helical segment and its relationship to biological potency of calcitonin analogs. , 2009, International journal of peptide and protein research.

[11]  C. Schmidt,et al.  Studies of synthetic peptide analogs of the amphipathic helix. Structure of complexes with dimyristoyl phosphatidylcholine. , 1985, The Journal of biological chemistry.

[12]  A. Argiolas,et al.  Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. , 1985, The Journal of biological chemistry.

[13]  E. Kaiser,et al.  Amphiphilic secondary structure: design of peptide hormones. , 1984, Science.

[14]  M. Phillips,et al.  The helical hydrophobic moments and surface activities of serum apolipoproteins. , 1983, Biochimica et biophysica acta.

[15]  R. Schwyzer,et al.  Liposome‐mediated labeling of adrenocorticotropin fragments parallels their biological activity , 1983, FEBS letters.

[16]  Mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: effect of lipid clusters on reaction rates. , 1982, Biophysical journal.

[17]  A. Gotto,et al.  Human plasma high density apolipoprotein A-I: effect of protein-protein interactions on the spontaneous formation of a lipid-protein recombinant. , 1981, Biochemical and biophysical research communications.

[18]  J. Segrest,et al.  Studies of synthetic peptide analogs of the amphipathic helix. Effect of charged amino acid residue topography on lipid affinity. , 1980, The Journal of biological chemistry.

[19]  R. Epand,et al.  Molecular interactions in the model lipoprotein complex formed between glucagon and dimyristoylglycerophosphocholine. , 1977, Biochemistry.

[20]  A. Gotto,et al.  Lipid-protein interactions in the plasma lipoproteins. , 1977, Biochimica et biophysica acta.

[21]  H. Hauser,et al.  Lateral compressibility and penetration into phospholipid monolayers and bilayer membranes , 1975, Nature.

[22]  A. Gotto,et al.  A molecular theory of lipid—protein interactions in the plasma lipoproteins , 1974, FEBS letters.

[23]  G. Fasman,et al.  Computed circular dichroism spectra for the evaluation of protein conformation. , 1969, Biochemistry.

[24]  C. E. Day,et al.  Molecular structure of serum lipoproteins. , 1969, Journal of theoretical biology.

[25]  M. Schiffer,et al.  Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. , 1967, Biophysical journal.

[26]  J. C. Kendrew,et al.  Structure and function of haemoglobin: II. Some relations between polypeptide chain configuration and amino acid sequence , 1965 .