Structural stability of amyloid beta 43 under different environmental conditions using simulated annealing and molecular dynamics simulation

• Main Authors: Yu-EnChou, 周佑恩
• Other Authors: Chi-Chuan Hwang
• Format: Others
• Language: zh-TW
• Published: 2013
• Online Access: http://ndltd.ncl.edu.tw/handle/18444423615983474660

碩士 === 國立成功大學 === 工程科學系碩博士班 === 101 === Amyloid beta(Aβ) is a major cause of Alzheimer's disease. There are three major forms of Aβ producing 40,42 and 43 residues long, accumulating and depositing in our brain forming protein amyloid plaques. Neuros would be damaged by this deposition.Accroding to the experiment in Alzheimer's disease, the previous researches show that the amyloid plaque of Aβ43 is more frequent and toxic than the other two, however, the structure of Aβ43 is not clear enough ,in order to expore this out. In this thesis, Aβ43 was simulated from 300K to 500K in aqueous solution under simulated annealing method. We select five possible candiates after the temperature drops to 300K. Sequentially, the five candiates were simulated under different pH values in room temperature during 80ns by using molecular dynamics. With the stable analysis of RMSD and Rg, we find out four probable conformers which has similar structural charasteristics of α-helix,segment 10-17, compared with Protein-Protein Interaction Energy and Principal component analysis in local minimum energy.These findings provide a data base for the future research.