Chapter 6 Modulation of Lipid Polymorphism by Peptides

Current Topics in Membranes and Transport

Volumn 44, Issue C, 1997, Pages 237-252

  Epand, Richard M ^a  

^a MCMASTER UNIVERSITY MEDICAL CENTRE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77956713445     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)60210-5     Document Type: Article

References (71)

1. Anantharamaiah G.M., Jones M.K., and Segrest J.P. An atlas of the amphipathic helical domains of human exchangeable plasma apolipoproteins. In: Epand R.M. (Ed). The Amphipathic Helix (1993), CRC Press, Boca Raton, FL. 109-142
2. Aranda F.J., Killian J.A., and de Kruijff B. Importance of the tryptophans of gramicidin for its lipid structure modulating activity in lysophosphatidylcholine and phosphatidylethanolamine model membranes. A comparative study employing gramicidin analogs and a synthetic alpha-helical hydrophobic polypeptide. Biochim. Biophys. Acta 901 (1987) 217-228
3. Batenburg A.M., and de Kruijff B. Modulation of membrane surface curvature by peptide-lipid interactions. Biosci. Rep. 8 (1988) 299-307
4. Ben-Efraim I., Strahilevitz J., Bach D., and Shai Y. Secondary structure and membrane localization of synthetic segments and a truncated form of the IsK (minK) protein. Biochemistry 33 (1994) 6966-6973
5. Brasseur A., Cabiaux V., Killian J.A., de Kruijff B., and Ruysschaert J.-M. Orientation of gramicidin A at the lysophosphatidylcholine/water interface: A serniempirical conformation analysis. Biochim. Biophys. Acta 855 (1986) 317-324
6. Callaghan R., van Gorkom L.C.M., and Epand R.M. A comparison of membrane properties and composition between cell lines selected and transfected for multi-drug resistance. Br. J. Cancer 66 (1992) 781-786
7. Casio M., and Wallace B.A. Conformation of alamethicin in phospholipid vesicles: Implications for insertion model. Proteins 4 (1988) 89-98
8. Challou N., Goormaghtigh E., Cabiaux V., Conrath K., and Ruysschaert J.-M. Sequence and structure of membrane-associated peptide of glycophorin A. Biochemistry 33 (1994) 6902-6910
9. Chernomordik L. Non-bilayer lipids and biological fusion intermediates. Chem. Phys. Lipids 81 (1996) 203-213
10. Colotto, A., and Epand, R. M. (1997). Structural study of the relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochemistry. Submitted for publication.
11. Colotto A., Lohner K., and Laggner P.J. Small-angle X-ray diffraction studies on the effects of melittin on lipid bilayer assemblies. Appl. Cryst. 24 (1991) 847-851
12. Cullis P.R., and de Kruijff B. Lipid polymorphism and the functional role of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
13. Cullis P.R., Hope M.L., and Tilcock C.P. Lipid polymorphism and the roles of lipids in membranes. Chem. Phys. Lipids 40 (1986) 127-144
14. de Kruijff B., and Cullis P.R. The influence of poly(L-lysine) on phospholipid polymorphism: Evidence that electrostatic polypeptide-phospholipid interactions can modulate bilayer/non-bilayer transitions. Biochim. Biophys. Acta 601 (1980) 235-240
15. Epand R.F., Martin I., Ruysschaert J.-M., and Epand R.M. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochem. Biophys. Res. Commun. 205 (1994) 1938-1943
16. Epand R.M. Diacylglycerols, lysolecithin, or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines. Biochemistry 24 (1985) 7092-7095
17. Epand R.M. Virus replication inhibitory peptide inhibits the conversion of phospholipid bilayers to the hexagonal phase. Biosci. Rep. 6 (1986) 647-653
18. Epand R.M. Biological consequences of alterations in the physical properties of membranes. In: Ohki S. (Ed). Cell and Model Membrane Interactions (1991), Plenum Press, New York 135-147
19. Epand R.M., and Epand R.F. Calorimetric detection of curvature strain in phospho-lipid bilayers. Biophys. J. 66 (1994) 1450-1456
20. Epand R.M., and Epand R.F. Relationship between the infectivity of influenza virus and the ability of its fusion peptide to perturb bilayers. Biochem. Biophys. Res. Commun. 202 (1994) 1420-1425
21. Epand R.M., and Polozov I. Liposomes and membrane stability. In: Barenholz Y., and Lasic D.D. (Eds). Nonmedical Applications of Liposomes (1996), CRC Press, Boca Raton, FL. 105-111
22. Epand R.M., Epand R.F., and McKenzie R.C. Effects of viral chemotherapeutic agents on membrane properties: Studies of cyclosporin A, benzyloxycarbonyl-D-Phe-L-Phe-Gly and amantadine. J. Biol. Chem. 262 (1987) 1526-1529
23. Epand R.M., Lobl T.J., and Renis H.E. Bilayer stab peptides and the inhibition of viral infection: Antimeasles activity of carbobenzoxy-Ser-Leu-amide. Biosci. Rep. 7 (1987) 745-749
24. Epand R.M., Stafford A.R., and Debanne M.T. Action of insulin in rat adipocytes and membrane properties. Biochemistry 30 (1991) 2092-2098
25. Epand R.M., Cheetham J.J., Epand R.F., Yeagle P.L., Richardson C.D., Rockwell A., and DeGrado W.F. Peptide models for the membrane destabilizing actions of viral fusion proteins. Biopolymers 32 (1992) 309-314
26. Epand R.M., Epand R.F., Richardson C.D., and Yeagle P.L. Structural requirements for the inhibition of membrane fusion by carbobenzoxy-D-Phe-Phe-Gly. Biochim. Biophys. Acta 1152 (1993) 128-134
27. Epand R.M., Stafford A., Leon B., Lock P.E., Tytler E.M., Segrest J.P., and Ananthara-maiah G.M. HDL and the apolipoprotein A-I protect erythrocytes against the generation of procoagulant activity. Arteriosclerosis Thrombosis 14 (1994) 1775-1783
28. Epand R.M., Shai Y., Segrest J.P., and Anantharamaiah G.M. Mechanism for the modulation of membrane bilayer properties by amphipathic helical peptides. Biopolymers 37 (1995) 319-338
29. 1H NMR Evidence for conformational heterogeneity in a voltage-gated peptide. Biochemistry 33 (1994) 4036-4045
30. Gething M.J., Doms R.W., York D., and White J. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell. Biol. 102 (1986) 11-23
31. Greathouse D.V., Hinton J.F., Kim K.S., and Koeppe II R.E. Gramidicin A/short-chain phospholipid dispersions: Chain length dependence of gramicidin conformation and lipid organization. Biochemistry 33 (1994) 4291-4299
32. Gruner S.M. Nonlamellar lipid phases. In: Yeagle P. (Ed). The Structure of Biological Membranes (1992), CRC Press, Boca Raton, FL. 211-250
33. Henderson R., Baldwin J.M., Ceska T.A., Zemlin F., Beckmann E., and Downing K.H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213 (1990) 899-929
34. Israelachvili J.N., Marcelja S., and Horn R.G. Physical principles of membrane organization. Q. Rev. Biophys. 13 (1980) 121-200
35. Janes N. Curvature stress and polymorphism in membranes. Chem. Phys. Lipids 81 (1996) 133-150
36. Kachel K., Asuncion-Punzalan E., and London E. Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: Parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids. Biochemistry 34 (1995) 15475-15479
37. Keller S.L., Bezrukov S.M., Gruner S.M., Tate M.W., Vodyanoy I., and Parsegian V.A. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys. J. 65 (1993) 23-27
38. Keller S.L., Gruner S.M., and Gawrisch K. Small concentrations of alamethicin induce cubic phase in bulk phosphatidylethanolamine mixtures. Biochim. Biophys. Acta 1278 (1996) 241-246
39. Kelsey D.R., Flanagan T.D., Young J.E., and Yeagle P.L. Inhibition of Sendai virus fusion with phospholipid vesicles and human erythrocyte membranes by hydrophobic peptides. Virology 182 (1991) 690-702
40. Kennedy S.J. Structures of membrane proteins. J. Membr. Biol. 42 (1978) 265-279
41. II phase induction by gramicidin in model membranes and its relation to channel formation. Biophys. J. 53 (1988) 111-117
42. II, phase formation by gramicidins A. B and C in dioleoylphosphatidylcholine model membranes: A study on the role of the tryptophan residues. Biochim. Biophys. Acta 897 (1987) 269-284
43. II, phase formation in phosphatidylcholine model membranes. Biochim. Biophys. Acta 978 (1989) 341-345
44. Killian J.A., Salemink I., de Planque M., Lindblom G., Koeppe II R.E., and Greathouse D.V. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmemhrane α-helical peptides: Importance of hydrophobic mismatch and proposed role of tryptophans. Biochemistry 35 (1996) 1037-1045
45. 2 terminus of influenza HA-2. J. Biol. Chem. 262 (1987) 6500-6505
46. Lohner K., and Epand R.M. Membrane interactions of hemolytic and antibacterial peptides. In: Bush C.A. (Ed). Advances in Biophysical Chemistry 6 (1997), JAI Press, Greenwich, CT. 53-66
47. Ludtke S.J., He K., Heller W.T., Harroun T.A., Yang L., and Huang H.W. Membrane pores induced by magainin. Biochemistry 35 (1996) 13723-13728
48. 2-terminal extremity of SIV/HIV fusogenic proteins. Biochim. Biophys. Acta 1240 (1995) 95-100
49. Martin I., Dubois M.-C., Saermark T., and Ruysschaert J.-M. Apolipoprotein A-I interacts with the N-terminal fusogenic domains of SIV (simian immunodeficiency virus) GP32 and HIV (human immunodeficiency virus) GP41: Implications in viral entry. Biochem. Biophys. Res. Commun. 186 (1992) 95-101
50. 2-terminal SIV fusion peptide into the lipid bilayer. FEBS Lett. 333 (1993) 325-330
51. Matsuzaki K., Murase O., Tokuda H., Funakoshi S., Fujii N., and Miyajima K. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 33 (1994) 3342-3349
52. Michel H. Three-dimensional crystals of a membrane protein complex. The photosyn-thetic reaction centre from Rhodopseudomonas viridis. J. Mol. Biol. 158 (1987) 567-572
53. Mishra V.K., Palgunachari M.N., Segrest J.P., and Anantharamaiah G.M. Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids: Evidence for the snorkel hypothesis. J. Biol. Chem. 269 (1994) 7185-7191
54. Mosior M., and McLaughlin S. Electrostatics and dimensionality can produce apparent cooperativity when protein kinase C and its substrates bind to acidic lipids in membranes. In: Lester D.S., and Epand R.M. (Eds). Protein Kinase C Current Concepts and Future Perspectives (1992), Ellis Horwood Ltd., Chichester, England 157-180
55. Muga A., Neugebauer W., Hirama T., and Surewicz W.K. Membrane interaction and conformational properties of the putative fusion peptide of PH-30, a protein active in sperm-egg fusion. Biochemistry 33 (1994) 4444-4448
56. Owens R.J., Anantharamaiah G.M., Kahlon J.B., Srinivas R.V., Compans R.W., and Segrest J.P. Apolipoprotin A-I and its amphipathic helix peptide analogues inhibit human immunodeficiency virus-induced syncytium formation. J. Clin. Invest. 86 (1990) 1142-1150
57. Polozov, I. V., Polozova, A. I., Tytler, E. M., Anantharamaiah, G. M., Segrest, J. P., Woolley, G. A., and Epand, R. M. (1997). Role of lipids in the permeabilization of membranes by class L amphipathic helical peptides. Biochemistry. In press.
58. Prosser R.S., and Davis J.H. Dynamics of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin. Biophys. J. 66 (1994) 1429-1440
59. 2H nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer. Biochemistry 30 (1991) 4687-4696
60. Prosser R.S., Daleman S.I., and Davis J.H. The structure of an integral membrane peptide: A deuterium NMR study of grarnicidin. Biophys. J. 66 (1994) 1415-1428
61. 2 viral polypeptides. Virology 105 (1980) 205-222
62. Segrest J.P., DeLoof H., Dohlman J.G., Brouilette C.G., and Anantharamaiah G.M. Amphipathic helix motif Classes and properties. Proteins 8 (1990) 103-117
63. Taraschi T.F., van der Steen A.T.M., de Kruijff B., Tellier C., and Verkleij A.J. Lectin-receptor interactions in liposomes: Evidence that binding of wheat germ agglutinin to glycoprotein-phosphatidylethanolamine vesicles induces nonbilayer structures. Biochemistry 21 (1982) 5756-5764
64. 2+ system. Eur. J. Biochem. 129 (1983) 621-625
65. II phase formation in dioleoylphosphatidylcholine model membranes. Biochim. Biophys. Acta 905 (1987) 222-226
66. II phase formation in erythrocyte membranes. Biochim. Biophys. Acta 946 (1988) 173-177
67. Tytler E.M., Segrest J.P., Epand R.M., Nie S.-Q., Epand R.F., Mishra V.K., Venkatachala-pathi Y.V., and Anantharamaiah G.M. Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes: Cross-sectional shapes of amphipathic α helixes control membrane stability. J. Biol. Chem. 268 (1993) 22112-22118
68. L,D helix. Proc. Natl. Acad. Sci. U.S.A. 68 (1971) 672-676
69. Voneche V., Portetelle D., Kettmann R., Willems L., Limbach K., Paoletti E., Ruysschaert J.M., Burny A., and Brasseur R. Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells. Proc. Natl. Acad. Science, U.S.A. 89 (1992) 3810-3814
70. White J. Membrane fusion. Science 258 (1992) 917-924
71. Wilson I.A., Skehel J.J., and Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature (London) 289 (1981) 366-373