Interaction of a β-sheet breaker peptide with lipid membranes

Journal of Peptide Science

Volumn 16, Issue 2, 2010, Pages 115-122

  Vitiello, Giuseppe ^a,b   Grimaldi, Manuela ^c   Ramunno, Anna ^c   Ortona, Ornella ^a,b   De Martino, Giovanni ^c   D'Ursi, Anna Maria ^c   D'Errico, Gerardino ^a,b  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b CSGI Consorzio per lo Sviluppo dei Sistemi a Grande Interfase   (Italy)

^c UNIVERSITY OF SALERNO   (Italy)

Author keywords

amyloid; sheet breaker; Electron spin resonance; Lipid bilayer; Spin label

Indexed keywords

AMPHOLYTE; BETA SHEET BREAKER PEPTIDE; CHOLESTEROL; DIOLEOYLPHOSPHATIDYLCHOLINE; MEMBRANE PHOSPHOLIPID; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; HYDROPHOBICITY; LIPID BILAYER; PARTITION COEFFICIENT; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; SOLUBILIZATION;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; HUMANS; MEMBRANE LIPIDS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS;

EID: 74749108240     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1207     Document Type: Article

References (57)

1. PrinceM,JacksonJ.WorldAlzheimerReport2009.Alzheimer's Disease International: London, 2009.
2. Katzman R, Jackson JE. Alzheimer disease: basic and clinical advances. J.Am. Geriatr. Soc. 1991; 39: 516-525.
3. Selkoe DJ. Alzheimer's disease: genotypes, phenotypes, and treatments. Science 1997; 275: 630-631.
4. Grundke-Iqbal I, Iqbal K, Quinlan M, Tung YC, Zaidi MS, Wisniewski HM. Microtubule-associated protein Tau. A component of Alzheimer paired helical filaments. J. Biol. Chem. 1986; 261: 6084-6089.
5. Hardy JL, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002; 297: 353-356.
6. Murphy MP, Hickman LJ, Eckman CB, Uljon SN, Wang R, Golde TE. γ -secretase,evidenceformultiple proteolyticactivitiesandinfluence of membrane positioning of substrate on generation of amyloid β peptides of varying length. J. Biol. Chem. 1999; 274: 11914-11923.
7. Seubert P, Vigo-Pelfrey C, Esch F, LeeM, Dovey H, Davis D, Sinha S, SchlossmacherM,Whaley J, Swindlehurst C,McCormack R, Wolfer R, Selkoe J, Lieberburg I, Schenk D. Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids. Nature 1992; 359: 325-327.
8. Stine WB, Dahigren KN, Krafft GA, LaDu MJ Jr. In vitro characterization of conditions for amyloid-peptide oligomerization and fibrillogenesis. J. Biol. Chem. 2003; 278: 11612-11622.
9. Vestergaard M, Kerman K, Masato S, Nagatani N, Takamura Y, Tamiya E. A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid β aggregation. J. Am. Chem. Soc. 2005; 127: 11892-11893.
10. Mclean CA, Cherny R, Fraser FW, Fuller SJ, Smith MJ, Beyreuther K, Bush AI, Masters CL. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann. Neurol. 1999; 46: 860-866.
11. Hsia AY, Masliah E, McConlogue L, Yu GQ, Tatsuno G, Hu K, Kholodenko D,Malenka RC,Nicoll RA, Mucke L. Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models. Proc. Natl. Acad. Sci. USA 1999; 96: 3228-3233.
12. Hartley DM, Walsh DM, Ye CP, Diehl T, Vasquez S, Vassilev PM, Teplow DB, Selkoe DJ. Protofibrillar intermediates of amyloid â-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical meurons. J. Neurosci. 1999; 19: 8876-8884.
13. Matsuzaki K.Physicochemical interactions of amyloid â-peptide with lipid bilayers. Biochim. Biophys. Acta 2007; 1768: 1935-1942.
14. Jarrett JT, Lansbury PT. Jr Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993; 73: 1055-1058.
15. Verdier Y, Zarandi M, Botond P. Amyloid β-peptide interactions with neuronal and glial cell plasma membrane: Binding and implications for Alzheimer's disease. J. Pept. Sci. 2004; 10: 229-248.
16. Ambroggio EE, Kim DH, Separovic F, Barrow CJ, Barnham KJ, Bagatolli LA, Fidelio GD. Surface behaviour and lipid interaction of Alzheimer β-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys. J. 2005; 88: 2706-2713.
17. Terzi E, Hölzemann G, Seelig J. Interaction of Alzheimer β-amyloid peptide (1-40) with lipid membranes. Biochemistry 1997; 36: 14845-14852.
18. Bokvist M, Lindström F, Watts A, Gröbner G. TwotypesofAlzheimer's β-amyloid (1-40) peptide membrane interactions: aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J.Mol. Biol. 2004; 335: 1039-1049.
19. Lindström F, Bokvist M, Sparrman T, Gröbner G. Association of amyloid-β peptide with membrane surfaces monitored by solid state NMR. Phys. Chem.Chem. Phys. 2002; 4: 5524-5530.
20. Lorenzo A, Yankner BA. β-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 1994; 91: 12243-12247.
21. MerliniG, AscariE, AmboldiN, Bellotti V, Arbustini E, Perfetti V, Ferrari M, Zorzoli I, Marinone MG, Garini P. Interaction of the anthracycline 4′-iodo-4′-deoxydoxorubicin with amyloid fibrils: inhibition of amyloidogenesis. Proc. Natl. Acad. Sci. USA 1995; 92: 2959-2963.
22. Tomiyama T, Shoji A, Kataoka K, Suwa Y, Asano S, Kaneko H, Endo N. Inhibition of amyloid β protein aggregation and neurotoxicity by rifampicin - Its possible function as a hydroxyl radical scavenger. J. Biol. Chem. 1996; 271: 6839-6844.
23. Kisilevsky R, Lemieux LJ, Fraser PE, Kong X, Hultin PG, Szarek WA. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: implications for Alzheimer's disease. Nat. Med. 1995; 1: 143-148.
24. Pappolla M, Bozner P, Soto C, Shao H, Robakis NK, Zagorski M, Frangione B, Ghiso J. Inhibition of Alzheimer β-fibrillogenesis by melatonin. J. Biol. Chem. 1998; 273: 7185-7188.
25. Tyernberg LO, Naslund J, Lindqvist F, Johansson J, Karlstrom AR, Thyberg J, Terenius L, Nordstedt C. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 1996; 271: 8545-8548.
26. Soto C, Sigurdsson EM, Morelli L, Kumar RA, Castano EM, Frangione B. β-Sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 1998; 4: 822-826.
27. Soto C. Plaque busters: strategies to inhibit amyloid formation in Alzheimer's disease. Mol. Med. Today 1999; 5: 343-350.
28. Chou PY, Fasman GD. Empirical predications of protein conformation. Annu. Rev. Biochem. 1978; 47: 251-276.
29. Kim CA, Berg JM. Thermodynamic β-sheet propensities measured using a zinc-finger host peptide. Nature 1993; 362: 267-270.
30. Wouters MA, Curmi PMG. An analysis of side chain interactions and pair correlations within antiparallel β-sheets: the differences between backbone hydrogen-bonded and nonhydrogen bonded residue pairs. Protein Sci. 1994; 3: 1992-1997.
31. Estrada LD, Soto C. Disrupting β-amyloid aggregation for Alzheimer disease treatment. Curr. Top. Med. Chem. 2007; 7: 115-126.
32. Adessi C, Soto C. Beta-sheet breaker strategy for the treatment of Alzheimer's disease. Drug Dev. Res. 2002; 56: 184-193.
33. Sigurdsson EM, Permanne B, Soto C, Wisniewski T, Frangione B. In vivo reversal of amyloid-β lesions in rat brain. J. Neuropathol. Exp. Neurol. 2000; 59: 11-17.
34. Permanne B, Adessi C, Fraga S, Frossard MJ, Saborio GP, Soto C. Are β-sheet breaker peptides dissolving the therapeutic problem of Alzheimer's disease?. J. Neural Transm. Suppl. 2002; 62: 293-301.
35. Permanne B, Adessi C, Saborio GP, Fraga S, Frossard MJ, Van Dorpe J, Dewachter I, Banks WA, Van Leuven F, Soto C. Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a β-sheet breaker peptide. FASEB J. 2002; 16: 860-862.
36. D'Errico G, Vitiello G, Ortona O, Tedeschi A, Ramunno A, D'Ursi AM. Interaction between Alzheimer's Aβ(25-35) peptide and phospholipid bilayers: The role of cholesterol. Biochim. Biophys. Acta 2008; 1778: 2710-2716.
37. Marsh D, Watts A. Spin-labeling and lipid-protein interactions in membranes. In Lipid-Protein Interactions, Vol. 2, Jost PC, GriffithOH (eds). Wiley Interscience: New York, 1982; 53-126.
38. Marsh D. Magnetic resonance of lipids and proteins in membranes. Curr. Opin. Colloid Interface Sci. 1997; 2: 4-14.
39. Powell JH, Johnson EM, Gannett PM. Improvement of a critical intermediate step in the synthesis of a nitroxide-based spin-labeled deoxythymidine analog. Molecules 2000; 5: 1244-1250.
40. Hankovszky HO, Hideg K, Lex L. Synthesis and reactions of highly reactive 1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-pyrrol-3-ylmethyl sulfonates. Synthesis 1980; 11: 914-916.
41. Mustafi D, Sosa-Peinado A, Gupta V, Gordon DJ, Makinen MW. Structure of spin-labeled methylmethanethiolsulfonate in solution and bound to TEM-1 b-lactamase determined by electron nuclear double resonance spectroscopy. Biochemistry 2002; 41: 797-808.
42. Shafer AM, Kalai T, Liu SQB, Hideg K, Voss JC. Site-specific insertion of spin-labeled L-amino acids in Xenopus Oocytes. Biochemistry 2004; 43: 8470-8482.
43. Karim CB, Zhang Z, Thomas DD. Synthesis of TOAC spin-labeled proteins and reconstitution in lipid membranes. Nat. Protoc. 2007; 2: 42-49.
44. Kivelson D. Theory of ESR linewidths of free radicals. J. Chem. Phys. 1960; 33: 1094-1106.
45. Tedeschi AM, Franco L, Ruzzi M, Paduano L, Corvaja C, D'Errico G. Micellar aggregation of alkyltrimethylammonium bromide surfactants studied by electron paramagnetic resonance of an anionic nitroxide. Phys. Chem. Chem. Phys. 2003; 5: 4204-4209.
46. Bates IR, Boggs JM, Feix JB, Harauz G. Membrane-anchoring and charge effects in the interaction of myelin basic protein with lipid bilayers studied by site-directed spin labeling. J. Biol. Chem. 2003; 278: 29041-29047.
47. Moser M, Marsh D, Meier P, Wassmer KH, Kothe G. Chain configuration and flexibility gradient in phospholipid membranes. Comparison between spin-label electron spin resonance and deuteron nuclear magnetic resonance, and identification of new conformations. Biophys. J. 1989; 55: 111-123.
48. Seelig J. Thermodynamics of lipid-peptide interactions. Biochim. Biophys. Acta 2004; 1666: 40-50.
49. Bhargava K, Feix JB. Membrane binding, structure, and localization of cecropin-mellitin hybrid peptides: a site-directed spin-labeling study. Biophys. J. 2004; 86: 329-336.
50. Swamy MJ, Marsh D. Spin-label electron spin resonance studies on the dynamics of the different phases of N-biotinylphosphatidylethanolamines. Biochemistry 1994; 33: 11656-11663.
51. Ramakrishnan M, Jensen PH, Marsh D. β-Synuclein association with phosphatidylglycerol probed by lipid spin labels. Biochemistry 2003; 42: 12919-12926.
52. D'Errico G, D'Ursi AM, Marsh D. Interaction of a peptide derived from glycoprotein gp36 of feline immunodeficiency virus and its lipoylated analogue with phospholipid membranes. Biochemistry 2008; 47: 5317-5327.
53. Davis JH, Clair JJ, Juhasz J. Phase equilibria in DOPC/DPPC d62/ Cholesterolmixtures. Biophys. J. 2009; 96: 521-539.
54. n oligopeptides. Macromolecules 1989; 22: 2939-2944.
55. MutterM, NefziA, SatoT, SunX, WahlF, WohrT. Pseudo-prolines (ψ Pro) for accessing "inaccessible" peptides. Pept. Res. 1995; 8: 145-153.
56. Wood JS, Wetzel R, Martin JD, Hurle MR. Prolines and amyloidogenicity in fragments of the Alzheimer's peptide β/A4. Biochemistry 1995; 34: 724-730.
57. Pistolesi S, Pogni R, Feix JB. Membrane insertion and bilayer perturbation by antimicrobial peptide CM15. Biophys. J. 2007; 93: 1651-1660.