Self-Assembly of Amyloid Beta Peptide Over Dialkoxy Disulfide Functionalized Nano Gold Colloidal Particles

Kazushige Yokoyama(1*), Amy L. Tran(2), Ronny Priefer(3)

(1) Department of Chemistry, The State University of New York College at Geneseo, One College Circle, Geneseo, NY 14454, USA, United States
(2) Department of Chemistry, The State University of New York College at Geneseo, One College Circle, Geneseo, NY 14454, USA, United States
(3) Department of Chemistry, Biochemistry, and Physics, Niagara University, Niagara University, NY 14109, USA, United States
(*) Corresponding author


DOI's assignment:
the author of the article can submit here a request for assignment of a DOI number to this resource!
Cost of the service: euros 10,00 (for a DOI)

Abstract


Aiming to more stably produce an oligomer form of amyloid beta (i.e., a key intermediate of fibrillogenesis which eventually leads to Alzheimer’s disease), the surface of gold colloids were functionalized with nitro-, phenyl-, chloro-, and methoxy-dibenzyloxy disulfide, and molecular interactions were investigated in a dimethyl sulfoxide environment. The transition of color change was observed at pHo as the pH value was lowered externally. As evidence of disulfide being adsorbed on the colloidal surface, the pHo values were dependent of each substituent of the dibenzyloxy disulfide compounds. The trend of pHo exhibited a parabolic relationship as a function of F-value (Swain-Lupton Field constant). Functionalization of gold colloidal surface with methoxy-dibenzyloxy disulfide achieved larger amplitude in repetitive peak shift between pH 4 and 10 implying a formation of an oligomer under the reversible process
Copyright © 2011 Praise Worthy Prize - All rights reserved.

Keywords


Amyloid Beta Peptide; Dibenzyloxy Disulfide; Gold Colloid; Alzheimer’s Disease

Full Text:

PDF


References


D. J. Selko The molecular pathology of Alzheimer's disease, Nuron 6 (1991) 487-498.

R. D. Terry Neuropathological changes in Alzheimer disease, Progress in Brain Research 101 (1994) 383-390.

G. G. Glenner and C. W. Wong Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochemical and Biophysical Research Communications 120 (1984) 885-890.

C. L. Masters, G. Simms, N. A. Weinman, G. Multhaup, B. L. McDonald and K. Beyreuther Amyloid Plaque core protein in Alzheimer disease and Down syndrome, Proceedings of the National Academy of Sciences of the United States of America 82 (1985) 4245-4249.

J. Rogers, N. R. Cooper, S. Webster, J. Schultz, P. L. McGeer, S. D. Styren, W. H. Civin, L. Brachova, B. Bradt and P. Ward Complement activation by beta-amyloid in Alzheimer disease, Proceedings of the National Academy of Sciences of the United States of America 89 (1992) 10016-10020.

C. L. Joachim, H. Mori and D. J. Selkoe Amyloid beta-protein deposition in tissues other than brain in Alzheimer's disease, Nature 341 (1989) 226-230.

J. P. Brion The pathology of the neuronal cytoskeleton in Alzheimer's disease, Biochimica et Biophysica Acta, 1160 (1992) 134-142.

H. Yamaguchi, Y. Nakazato, S. Hirai, M. Shoji and Y. Harigaya Electron micrograph of diffuse plaques. Initial stage of senile plaque formation in the Alzheimer brain, American Journal of Pathology 135 (1989) 593-597.

J. T. Jarrett, E. P. Berger and J. Lansbury, P. T. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease, Biochemistry 32 (1993) 4693-4697.

M. Shoji, T. E. Golde, J. Ghiso, T. T. Cheung, S. Estus, L. M. Shaffer, X. D. Cai, D. M. McKay, R. Tinter, B. Frangione and S. G. Younkin Production of the Alzheimer amyloid beta protein by normal proteolytic processing, Science 258 (1992) 126-129.

P. Seubert, C. Vigo-Pelfrey, F. Esch, M. Lee, H. Dovey, D. Davis, S. Sinha, M. Schlossmacher, J. Whaley, C. Swindlehurst, R. McCormac, R. Wolfert, D. J. Selkoe, I. Lieberburg and D. Schenk Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids, Nature 359 (1992) 325-327.

D. M. Walsh, A. Lomakin, G. B. Benedek, M. M. Condron and D. B. Teplow, Amyloid -protein fibrillogenesis, J. Biol. Chem. 272 (1997) 22364 - 22372.

A. Lomakin, D. S. Chung, G. B. Benedek, D. A. Kirshner and D. B. Teplow On the nucleation and growth of amyloid -protein fibrils: detection of nuclei and quantitation of rate constants, Proc. Natl. Acad. Sci. USA. 93 (1996) 1125-1129.

D. A. Kirschner, H. Inouye, L. K. Duffy, A. Sinclair, M. Lind and D. J. Selkoe Synthetic peptide homologous to .beta. protein from Alzheimer disease forms amyloid-like fibrils in vitro, Proc. Natl. Acad .Sci. U S A 84 (1987) 6953-6957.

M. P. Lambert, A. K. Barlow, B. A. Chromy, C. Edwards, R. Freed, M. Liosatos, T. E. Morgan, I. Rozovsky, B. Trommer, K. L. Viola, P. Wals, C. Zhang, C. E. Finch, G. A. Krafft and W. L. Klein Diffusible, nonfibrillar ligands derived from A 1-42 are potent central nervous system neurotoxins, Proc. Natl. Acad. Sci. U S A 95 (1998) 6448-6453.

D. M. Walsh, I. Klyubin, J. V. Fadeeva, W. K. Cullen, R. Anwyl, M. S. Wolfe, M. J. Rowan and D. J. Selko Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo, Nature 416 (2002) 535-539.

M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formigli, J. Zurdo, N. Taddei, G. Ramponi, C.M. Dobson and M. Stefani Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases, Nature 416 (2002) 507-511.

K. Yokoyama Modeling of Reversible Protein Conjugation on Nanoscale Surface, in: S.M. Musa (Ed.), Computational Nanotechnology: Modeling and Applications with MATLAB, CRC Press-Taylor and Francis Group, LLC, 2011.

K. Yokoyama Nanoscale Surface Size Dependence in Protein Conjugation, in: E.J. Chen and N. Peng (Eds.), Advances in Nanotechnology, Nova Publisher, 2010, pp. 65-104.

K. Yokoyama, N. M. Briglio, D. Sri Hartati, S. M. W. Tsang, J. E. MacCormac and D. R. Welchons Nanoscale size dependence in the conjugation of amyloid beta and ovalbumin proteins on the surface of gold colloidal particles, Nanotechnology 19 (2008) 375101-375108.

K. Yokoyama, N. B. Gaulin, H. Cho and N. M. Briglio Temperature Dependence of Conjugation of Amyloid Beta Peptide on the Gold Colloidal Nanoparticles, Journal of Physical Chemistry A 114 (2010) 1521-1528.

R. Priefer, Y. J. Lee, F. Barrios, J. H. Wosnick, A.-M. Lebuis, P. G. Farrell, D. N. Harpp, A. Sun, S. Wu and J. P. Snyder J. Am. Chem. Soc. 124 (2002) 5626.

R. R. Fraser, G. Boussard, J. K. Saunders and J. B. Lambert, J. Am. Chem. Soc. 93 (1971) 3822.

H. Kessler and W. Rundel Chem. Ber. 101 (1968) 3350.

T. Koritsanszky, J. Buschmann, P. Luger, H. Schmidt and R. Steudel J. Phys. Chem. 98 (1994) 5416.

R. Borghi, L. Lunazzi, G. Placucci, G. Cerioni, E. Foresti and A.J. Plumitallo Org. Chem. Biol. 62 (1997) 4924.

E. Zysman-Colman and D.N. Harpp J. Org. Chem. 70 (2005) 5964.

D.M. Rudzinski and R. Priefer Tetrahedron Letters 50 (2009) 1629–1632.

K. Yokoyama and D.R. Welchons The conjugation of amyloid beta protein on the gold colloidal nanoparticles' surfaces, Nanotechnology 18 (2007) 105101-105107.

S. Link and M. El-Sayed Spectral properties and relaxation dynamics of surface plasmon electronic oscillations in gold and silver nanodots and nanorods, J. Phys. Chem. B 103 (1999) 8410-8426.

K. L. Kelly, E. Coronado, L. L. Zhao and G. C. Schatz The optical properties of metal nanoparticles: the influence of size, shape, and dielectric environment, J. Phys. Chem. B 107 (2003) 668-677.

T. R. Jensen, G. C. Schatz and R. P. Van Duyne Nanosphere lithography: surface plasmon resonance spectrum of a periodic array of silver nanoparticles by ultraviolet-visible extinction spectroscopy and electrodynamic modeling, J. Phys. Chem. B 103 (1999) 2394-2401.

C. G. Swain and E. C. Lupton Field Resonance Components of Substituent Effects, J Am Chem Soc 90 (1968) 4328-4337.

D. B. Carter and K. C. Chou A model for structure-dependent binding of Congo red to Alzheimer beta-amyloids, Neurobiol Aging 19 (1998) 37-40.

A. Melquiond, X. Dong, N. Mousseau and P. Derreumaux Curr. Alzheimer Res. 5 (2008) 244.


Refbacks

  • There are currently no refbacks.



Please send any question about this web site to info@praiseworthyprize.com
Copyright © 2005-2020 Praise Worthy Prize