Simulation Study of Circumstantial Factors on Behavior of Amyloid Peptide in Alzheimer's Disease

Sang Wook Kim; Young Wook Song; Mi Ja Shim

Journal of Industrial and Engineering Chemistry, Vol.7, No.1, 7-10, January, 2001

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Simulation Study of Circumstantial Factors on Behavior of Amyloid Peptide in Alzheimer's Disease

Sang Wook Kim, Young Wook Song, and Mi Ja Shim^{1, †}

Department of Chemical Engineering, The University of Seoul, Seoul 130-743, Korea
¹Department of Life Science, The University of Seoul, Seoul 130-743, Korea

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The effects of circumstantial factors on β-amyloid peptide (β-AP) behavior, penetration, and aggregation were studied using cellular automata (CAs). To identify the mechanisms and relationships between the factors and the resulting behavior, β-AP was simulated using over-critical, and under-critical conditions. In the case of the simulation using over-critical conditions, the β-AP penetrated and aggregated on the surface of the lipid membrane. However, when β-AP was simulated using under-critical conditions, it did not aggregate but only penetrated the surface of the lipid membrane. From the simulation results, circumstantial factors such as pH, oligomer concentration, and solubility were all found to have an important effect on beta -AP behavior.

Keywords:β-Amyloid Peptide (β-AP);Cellular Automata (CAs);pH;Solubility;Oligomer Concentration

[References]

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[Referenced By]

[1] Selkoe DJ, Science, 275(5300), 630 (1997)

[2] Pillot T, Goethals M, Vanloo B, Talussot C, Brasseur R, Vandekerckhove J, Rosseneu M, Lins L, J. Biol. Chem., 271, 28757 (1996)

[3] El-Agnaf OMA, Eur. J. Biochem., 258, 157 (1998)

[4] Ma K, Clancy EL, Zhang YB, Ray DG, Wollenberg K, Zagorski MG, J. Am. Chem. Soc., 121(38), 8698 (1999)

[5] Burks C, Farmer D, Physica, 10D, 157 (1984)

[6] Oono Y, Kohmoto M, Phys. Rev. Lett., 55, 2927 (1985)

[7] Dubois DM, Biosys., 43, 97 (1997)

[8] Laboz-Beltra R, Biosys., 44, 209 (1997)

[9] Killingback T, Doebeli M, J. Theor. Biol., 191, 335 (1998)

[10] Keymer JE, Marquet PA, Johnson AR, J. Theor. Biol., 194, 79 (1998)

[11] Song YW, Shim MJ, Kim SW, J. Ind. Eng. Chem., 5(4), 302 (1999)

[12] Harper JD, Lansbury PT, Annu. Rev. Biochem., 66, 385 (1997)

[13] Terzi E, Holzemann G, Seelig J, Biochem., 36, 14845 (1997)

[14] Terzi E, Holzemann G, Seelig J, J. Mol. Biol., 252, 633 (1995)

[15] Tjernberg LO, Callaway DJE, Tjernberg A, Hahne S, Lilliehook C, Terenius L, Thyberg J, Nordstedt C, J. Biol. Chem., 274, 12619 (1999)

[16] Marcinowski KJ, Shao H, Clancy EL, Zagorski MG, J. Am. Chem. Soc., 120(43), 11082 (1998)

[17] Lazo ND, Downing DT, J. Peptide Res., 53, 633 (1999)