Abstract: In order to suppress the transformation of amyloid β polypeptide (Aβ)  from random curling or α-helix to β-folding structure, we studied the conformational changes of wild type Aβ and its array mutants. Combining Markov model and molecular dynamics simulation, we studied the conformational change precess  of the wild type,  A4 type and D7N type Aβ, and identified the  conformational transformation path of three Aβ types. The experimental results show that one region of β-folding is found in the wild type Aβ, and the conformation of the A4 type Aβ is almost unchanged, while two regions of β-folding are found in the D7N type Aβ, indicating that the D7N type mutant has the characteristic of promoting β-folding. The results provide a theoretical baisis for exploring treatment methods for Alzheimer’s disease.

Key words: Alzheimer’s disease,  , amyloid β polypeptide,  , molecular dynamics simulation,  , Markov model