Effect of curcumin-associated and lipid ligand-functionalized nanoliposomes on aggregation of the Alzheimer's Aβ peptide

Nanomedicine: Nanotechnology, Biology, and Medicine

Volumn 7, Issue 5, 2011, Pages 541-550

  Taylor, Mark ^a   Moore, Susan ^a   Mourtas, Spyridon ^b   Niarakis, Anna ^b   Re, Francesca ^c   Zona, Cristiano ^c   Ferla, Barbara La ^c   Nicotra, Francesco ^c   Masserini, Massimo ^c   Antimisiaris, Sophia G ^b,d   Gregori, Maria ^c   Allsop, David ^a  

^a LANCASTER UNIVERSITY   (United Kingdom)

^b UNIVERSITY OF PATRAS   (Greece)

^c UNIVERSITY OF MILANO BICOCCA   (Italy)

^d INSTITUTE OF CHEMICAL ENGINEERING SCIENCES   (Greece)

Author keywords

Amyloid ; Curcumin; Fibril; Liposomes; Oligomer

Indexed keywords

ALZHEIMER; ALZHEIMER'S DISEASE; CARDIOLIPINS; CLICK CHEMISTRY; CURCUMIN; CURCUMIN DERIVATIVES; FIBRIL; IN-VITRO; LIPID PHASE; NANOLIPOSOMES; PHOSPHATIDIC ACIDS;

GLYCOPROTEINS; LIGANDS; LIPOSOMES; NEURODEGENERATIVE DISEASES; OLIGOMERS; PEPTIDES;

PHOSPHOLIPIDS;

AMYLOID BETA PROTEIN[1-42]; CARDIOLIPIN; CURCUMIN; CURCUMIN DERIVATIVE; GANGLIOSIDE GM1; LIPOSOME; NANOLIPOSOME; PHOSPHATIDIC ACID; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; ARTICLE; DRUG EFFECT; LIPID ANALYSIS; PROTEIN AGGREGATION; PROTEIN DETERMINATION;

ALZHEIMER DISEASE; AMYLOID BETA-PEPTIDES; CARDIOLIPINS; CURCUMIN; G(M1) GANGLIOSIDE; HUMANS; LIGANDS; LIPOSOMES; NANOPARTICLES; PEPTIDE FRAGMENTS; PHOSPHATIDIC ACIDS;

EID: 80053216654     PISSN: 15499634     EISSN: 15499642     Source Type: Journal    
DOI: 10.1016/j.nano.2011.06.015     Document Type: Article

References (45)

1. Brookmeyer R., Gray S., Kawas C. Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am J Public Health 1998, 88:1337-1342.
2. American Health Assistance Foundation Alzheimer disease research: about Alzheimer Available from:. http://www.ahaf.org/alzheimers/about/.
3. Brookmeyer R., Corrada M.M., Curriero F.C., Kawas C. Survival following a diagnosis of Alzheimer disease. Arch Neurol 2002, 59:1764-1767.
4. Citron M. Alzheimer's disease: strategies for disease modification. Nat Rev Drug Discov 2010, 9:387-398.
5. Hardy J., Allsop D. Amyloid deposition as the central event in the aetiology of Alzheimer's disease. Trends Pharmacol Sci 1991, 12:383-388.
6. Mann D.M., Iwatsubo T., Ihara Y., Cairns N.J., Lantos P.L., Bogdanovic N., et al. Predominant deposition of amyloid-β 42(43) in plaques in cases of Alzheimer's disease and hereditary cerebral hemorrhage associated with mutations in the amyloid precursor protein gene. Am J Pathol 1996, 148:1257-1266.
7. Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
8. Siemers E., DeMattos R.B., May P.C., Dean R.A. Role of biochemical Alzheimer's disease biomarkers as end points in clinical trials. Biomark Med 2010, 4:81-89.
9. Yin Y.I., Bassit B., Zhu L., Yang X., Wang C. Li YM. γ-Secretase substrate concentration modulates the Aβ42/Aβ40 ratio: implications for Alzheimer disease. J Biol Chem 2007, 282:23639-23644.
10. Shen Y., Yu L.C. Potential protection of curcumin against hypoxia-induced decreases in β-III tubulin content in rat prefrontal cortical neurons. Neurochem Res 2008, 33:2112-2117.
11. Thomas T., Nadackal T.G., Thomas K. Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation. Neuroreport 2001, 12:3263-3267.
12. Ono K., Hasegawa K., Naiki H., Yamada M. Curcumin has potent anti-amyloidogenic effects for Alzheimer's β-amyloid fibrils in vitro. J Neurosci Res 2004, M75:742-750.
13. Kim H., Park B.S., Lee K.G., Choi C.Y., Jang S.S., Kim Y.H., et al. Effects of naturally occurring compounds on fibril formation and oxidative stress of β-amyloid. J Agric Food Chem 2005, 53:8537-8541.
14. Yang F., Lim G.P., Begum A.N., Ubeda O.J., Simmons M.R., Ambegaokar S.S., et al. Curcumin inhibits formation of amyloid β oligomers and fibrils, binds plaques, and reduces amyloid in vivo. J Biol Chem 2005, 280:5892-5901.
15. Kim D.S., Park S.Y., Kim J.K. Curcuminoids from Curcuma longa L. (Zingiberaceae) that protect PC12 rat pheochromocytoma and normal human umbilical vein endothelial cells from βA(1-42) insult. Neurosci Lett 2001, 303:57-61.
16. Re F., Airoldi C., Zona C., Masserini M., La Ferla B., Quattrocchi N., et al. β-Amyloid aggregation inhibitors: small molecules as candidate drugs for therapy of Alzheimer's disease. Curr Med Chem 2010, 17:2990-3006.
17. Anand P., Thomas S.G., Kunnumakkara A.B., Sundaram C., Harikumar K.B., Sung B., et al. Biological activities of curcumin and its analogues (congeners) made by man and mother nature. Biochem Pharmacol 2008, 76:1590-1611.
18. Bernabe-Pineda M., Ramirez-Silva M.T., Romero-Romo M., Gonzalez-Vergara E., Rojas-Hernandez A. Determination of acidity constants of curcumin in aqueous solution and apparent rate constant of its decomposition. Spectrochim Acta A Mol Biomol Spectrosc 2004, 60:1091-1097.
19. Wang Y.J., Pan M.H., Cheng A.L., Lin L.I., Ho Y.S., Hsieh C.Y., et al. Stability of curcumin in buffer solutions and characterization of its degradation products. J Pharm Biomed Anal 1997, 15:1867-1876.
20. Tonnesen H.H., Karlsen J. Studies on curcumin and curcuminoids. VI. Kinetics of curcumin degradation in aqueous solution. Z Lebensm Unters Forsch 1985, 180:402-404.
21. Montet X., Funovics M., Montet-Abou K., Weissleder R., Josephson L. Multivalent effects of RGD peptides obtained by nanoparticle display. J Med Chem 2006, 49:6087-6093.
22. Hong S., Leroueil P.R., Majoros I.J., Orr B.G., Baker J.R., Banaszak Holl M.M. The binding avidity of a nanoparticle-based multivalent targeted drug delivery platform. Chem Biol 2007, 14:107-115.
23. Tassa C., Duffner J.L., Lewis T.A., Weissleder R., Schreiber S.L., Koehler A.N., et al. Binding affinity and kinetic analysis of targeted small molecule-modified nanoparticles. Bioconjug Chem 2010, 21:14-19.
24. Antimisiaris S.G., Kallinteri P., Fatouros D. Liposomes and drug delivery. Pharmaceutical manufacturing handbook production and processes 2008, 443-533. John Wiley & Sons, New York. S.C. Gad (Ed.).
25. Mourtas S., Canovi M., Zona C., Aurilia D., Niarakis A., La Ferla B., et al. Curcumin-decorated nanoliposomes with very high affinity for amyloid-β1-42 peptide. Biomaterials 2011, 32:1635-1645.
26. Matsuzaki K. Physicochemical interactions of amyloid β-peptide with lipid bilayers. Biochim Biophys Acta 2007, 1768:1935-1942.
27. Chauhan A., Ray I., Chauhan V.P. Interaction of amyloid β-protein with anionic phospholipids: possible involvement of Lys28 and C-terminus aliphatic amino acids. Neurochem Res 2000, 25:423-429.
28. McLaurin J., Chakrabartty A. Membrane disruption by Alzheimer β-amyloid peptides mediated through specific binding to either phospholipids or gangliosides. Implications for neurotoxicity. J Biol Chem 1996, 271:26482-26489.
29. Kakio A., Nishimoto S.I., Yanagisawa K., Kozutsumii Y., Matsuzaki K. Cholesterol-dependent formation of GM1 ganglioside-bound amyloid β-protein, an endogenous seed for Alzheimer amyloid. J Biol Chem 2001, 276:24985-24990.
30. Aisenbrey C., Bechinger B., Gröbner G. Macromolecular crowding at membrane interfaces: adsorption and alignment of membrane peptides. J Mol Biol 2008, 375:376-385.
31. Yanagisawa K. Role of gangliosides in Alzheimer's disease. Biochim Biophys Acta 2007, 1768:1943-1951.
32. Gobbi M., Re F., Canovi M., Beeg M., Gregori M., Sesana S., et al. Lipid-based nanoparticles with high binding affinity for amyloid-β1-42 peptide. Biomaterials 2010, 31:6519-6529.
33. Taylor M., Moore S., Mayes J., Parkin E., Beeg M., Canovi M., et al. Development of a proteolytically stable retro-inverso peptide inhibitor of β-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. Biochemistry 2010, 49:3261-3272.
34. Kokona M., Kallinteri P., Fatouros D., Antimisiaris S.G. Stability of SUV liposomes in the presence of cholate salts and pancreatic lipases: effect of lipid composition. Eur J Pharm Sci 2000, 9:245-252.
35. Hassane F., Frisch B. Schuber F. Targeted liposomes: convenient coupling of ligands to preformed vesicles using "click chemistry". Bioconjug Chem. 2006, 17:849-854.
36. Usta M., Wortelboer H.M., Vervoort J., Boersma M.G., Rietjens I.M., van Bladeren P.J., et al. Human glutathione S-transferase-mediated glutathione conjugation of curcumin and efflux of these conjugates in Caco-2 cells. Chem Res Toxicol 2007, 20:1895-1902.
37. Stewart J.C.M. Colorimetric determination of phospholipids with ammonium ferrothiocyanate. Anal Biochem 1980, 104:10-14.
38. Zhang L., Rozek A., Hancock R.E. Interaction of cationic antimicrobial peptides with model membranes. J Biol Chem 2001, 276:35714-35722.
39. Manzoni C., Colombo L., Messa M., Cagnotto A., Cantu L., Del Favero E., et al. Overcoming synthetic Aβ peptide aging: a new approach to an age-old problem. Amyloid 2009, 16:71-80.
40. Ray B., Bisht S., Maitra A., Maitra A., Lahiri D.K. Neuroprotective and neurorescue effects of a novel polymeric nanoparticle formulation of curcumin (NanoCurc) in the neuronal cell culture and animal model: implications for Alzheimer's disease. J Alzheimer's Dis 2011, 23:61-77.
41. Mulik R.S., Mönkkönen J., Juvonen R.O., Mahadik K.R., Paradkar A.R. ApoE3 mediated poly(butyl) cyanoacrylate nanoparticles containing curcumin: study of enhanced activity of curcumin against β amyloid induced cytotoxicity using in vitro cell culture model. Mol Pharm 2010, 7:815-825.
42. Saraiva A.M., Cardoso I., Pereira M.C., Coelho M.A., Saraiva M.J., Möhwald H., et al. Controlling amyloid-β peptide(1-42) oligomerization and toxicity by fluorinated nanoparticles. Chembiochem 2010, 11:1905-1913.
43. Liu G., Men P., Kudo W., Perry G., Smith M.A. Nanoparticle-chelator conjugates as inhibitors of amyloid-β aggregation and neurotoxicity: a novel therapeutic approach for Alzheimer disease. Neurosci Lett 2009, 455:187-190.
44. Saraiva A.M., Cardoso I., Saraiva M.J., Tauer K., Pereira M.C., Coelho M.A., et al. Randomization of amyloid-β-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity. Macromol Biosci 2010, 10:1152-1163.
45. Muhs A., Hickman D.T., Pihlgren M., Chuard N., Giriens V., Meerschman C., et al. Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice. Proc Natl Acad Sci USA 2007, 104:9810-9815.