Inhibition of beta 1-40 amyloid fibrillation with N-acetyl-l-cysteine capped quantum dots

Biomaterials

Volumn 31, Issue 1, 2010, Pages 91-98

  Xiao, Lehui ^a,b   Zhao, Dan ^a   Chan, Wing Hong ^a   Choi, Martin M F ^a   Li, Hung Wing ^a  

^a HONG KONG BAPTIST UNIVERSITY   (Hong Kong)

^b Key Laboratory for Bio Nanotechnology and Molecular Engineering of Hunan Province   (China)

Author keywords

Nanoparticle; Peptide; Self assembly; TEM (transmission electron microscopy)

Indexed keywords

ALZHEIMER'S DISEASE; AMYLOID FIBRIL; AMYLOID PEPTIDES; CONCENTRATION DEPENDENCE; ELONGATION PROCESS; FIBRIL GROWTH; HYDROGEN BONDINGS; INHIBITION EFFECT; LOW CONCENTRATIONS; N-ACETYL L-CYSTEINE; PRIMARY FACTORS; PROTOFIBRILS; QUANTUM DOT; SELF-ASSEMBLE; TEM (TRANSMISSION ELECTRON MICROSCOPY); WATER-DISPERSED;

AMINES; CONCENTRATION (PROCESS); GLYCOPROTEINS; HYDROGEN; HYDROGEN BONDS; NANOPARTICLES; OLIGOMERS; PEPTIDES; QUENCHING; SELF ASSEMBLY; TRANSMISSION ELECTRON MICROSCOPY;

SEMICONDUCTOR QUANTUM DOTS;

ACETYLCYSTEINE; AMYLOID BETA PROTEIN[1-40]; GLYCYLGLYCINE; PHOSPHATE BUFFERED SALINE; QUANTUM DOT; THIOFLAVINE;

ARTICLE; BINDING KINETICS; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG DELIVERY SYSTEM; DRUG MECHANISM; FLUORESCENCE IMAGING; GROWTH INHIBITION; HYDRODYNAMICS; INHIBITION KINETICS; LIGHT SCATTERING; MATHEMATICAL MODEL; MOLECULAR INTERACTION; PARTICLE SIZE; PRIORITY JOURNAL; TRANSMISSION ELECTRON MICROSCOPY;

ACETYLCYSTEINE; AMYLOID BETA-PROTEIN; FLUORESCENT DYES; KINETICS; MICROSCOPY, ELECTRON, TRANSMISSION; MICROSCOPY, FLUORESCENCE; PEPTIDE FRAGMENTS; QUANTUM DOTS; THIAZOLES;

EID: 70350348150     PISSN: 01429612     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2009.09.014     Document Type: Article

References (34)

1. Caughey B., Peter T., and Lansbury J. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregation from the innocent bystanders. Annu Rev Neurosci 26 (2003) 267-298
2. Pepys M.B. Amyloidosis. Annu Rev Med 57 (2006) 223-241
3. Cohen F.E., and Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature 426 (2003) 905-909
4. Soto C., Sigurdsson E.M., Modelli L., Kumar R.A., Castano E.M., and Frangione B. β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat Med 4 (1998) 822-826
5. Lieo A., Greenberg S.M., and Growdon J.H. Current pharmacotherapy for Alzheimer's disease. Annu Rev Med 57 (2006) 513-533
6. Georganopoulou D.G., Chang L., Nam J.M., Thaxton C.S., Mufson E.J., Klein W.L., et al. Nanoparticle-based detection in cerebral spinal fluid of a soluble pathogenic biomarker for Alzheimer's disease. Proc Natl Acad Sci U S A 102 (2005) 2273-2276
7. Haes A.J., Hall W.P., Chang L., Klein W.L., and Duyne R.P.V. A localized surface plasmon resonance biosensor: first steps toward an assay for Alzheimer's disease. Nano Lett 4 (2004) 1029-1034
8. Kogan M.J., Bastus N.G., Amigo R., Grillo-Bosch D., Araya E., Turiel A., et al. Nanoparticle-mediated local and remote manipulation of protein aggregation. Nano Lett 6 (2006) 110-115
9. Linse S., Cabaleiro-Lago C., Xue W.F., Lynch I., Lindman S., Thulin E., et al. Nucleation of protein fibrillation by nanoparticles. Proc Natl Acad Sci U S A 104 (2007) 8691-8696
10. 2 nanoparticles promote β-amyloid fibrillation in vitro. Biochem Biophys Res Commun 373 (2008) 315-318
11. Cabaleiro-Lago C., Quinlan-Pluck F., Lynch I., Lindman S., Minogue A.M., Thulin E., et al. Inhibition of amyloid β protein fibrillation by polymeric nanoparticles. J Am Chem Soc 130 (2008) 15437-15443
12. Liu G., Garrett M.R., Men P., Zhu X., Perry G., and Smith M.A. Nanoparticle and other metal chelation therapeutics in Alzheimer disease. Biochim Biophys Acta 1741 (2005) 246-252
13. Zhang H., Wang L., Xiong H., Hu L., Yang B., and Li W. Hydrothermal synthesis for high-quality CdTe nanocrystals. Adv Mater 15 (2003) 1712-1715
14. Yu W.W., Qu L., Guo W., and Peng X. Experimental determination of the extinction coefficient of CdTe, CdSe, and CdS nanocrystals. Chem Mater 15 (2003) 2854-2860
15. Ban T., Hamada D., Hasegawa K., Naiki H., and Goto Y. Direct Observation of amyloid fibril growth monitored by thioflavin T fluorescence. J Biol Chem 278 (2003) 16462-16465
16. Hasegawa K., Yamaguchi I., Omata S., Gejyo F., and Naiki H. Interaction between Aβ(1-42) and Aβ(1-40) in Alzheimer's β-amyloid fibril formation in vitro. Biochemistry 38 (1999) 15514-15521
17. Naiki H., Higuchi K., Hosokawa M., and Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T. Anal Biochem 177 (1989) 244-249
18. Jarrett J.T., Peter T., and Lansbury J. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie?. Cell 73 (1993) 1055-1058
19. Lomakin A., Chung D.S., Benedek G.B., Kirschner D.A., and Teplow D.B. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci U S A 93 (1996) 1125-1129
20. Massi F., and Straub J.E. Energy landscape theory for Alzheimer's amyloid β-peptide fibril elongation. Proteins Struct Funct Genet 42 (2001) 217-229
21. Tomski S.J., and Murphy R.M. Kinetics of aggregation of synthetic β-amyloid peptide. Arch Biochem Biophys 294 (1992) 630-638
22. Yagi H., Ban T., Morigaki K., Naiki H., and Goto Y. Visualization and classification of amyloid β supramolecular assemblies. Biochemistry 46 (2007) 15009-15017
23. Ban T., Morigaki K., Yagi H., Kawasaki T., Kobayashi A., Yuba S., et al. Real-time and single fibril observation of the formation of amyloid β spherulitic structures. J Biol Chem 281 (2006) 33677-33683
24. Lomakin A., Teplow D.B., Kirschner D.A., and Benedek G.B. Kinetic theory of fibrillogenesis of amyloid β-protein. Proc Natl Acad Sci U S A 94 (1997) 7942-7947
25. Nielsen L., Khurana R., Coats A., Frokjaer S., Brange J., Vyas S., et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40 (2001) 6036-6046
26. Ban T., Hoshino M., Takahashi S., Hamada D., Hasegawa K., Naiki H., et al. Direct observation of Ab amyloid fibril growth and inhibition. J Mol Biol 344 (2004) 757-767
27. Nguyen P.H., Li M.S., Stock G., Straub J.E., and Thirumalai D. Monomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock-lock mechanism. Proc Natl Acad Sci U S A 104 (2006) 111-116
28. Esler W.P., Stimson E.R., Jennings J.M., Vinters H.V., Ghilardi J.R., Lee J.P., et al. Alzheimer's disease amyloid propagation by a template-dependent dock-lock mechanism. Biochemistry 39 (2000) 6288-6295
29. Kloepfer J.A., Mielke R.E., and Nadeau J.L. Uptake of CdSe and CdSe/ZnS quantum dots into bacterial via purine-dependent mechanisms. Appl Environ Microbiol 71 (2005) 2548-2557
30. Kusumoto Y., Lomakin A., Teplow D.B., and Benedek G.B. Temperature dependence of amyloid β-protein fibrillization. Proc Natl Acad Sci U S A 95 (1998) 12277-12282
31. Hill T.L. Length dependence of rate constants for end-to-end association and dissociation of equilibrium linear aggregates. Biophys J 44 (1983) 285-288
32. Guinnup D.E., and Schultz J.S. Investigation of aggregation kinetics via laser light scattering. J Phys Chem 90 (1986) 3282-3288
33. Grunwald D., Hoekstra A., Dange T., Buschmann V., and Kubitscheck U. Direct observation of single protein molecules in aqueous solution. ChemPhysChem 7 (2006) 812-815
34. Liedl T., Keller S., Simmel F.C., Radler J.O., and Parak W.J. Fluorescent nanocrystals as colloidal probes in complex fluids measured by fluorescence correlation spectroscopy. Small 1 (2005) 997-1003