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128th General Meeting of Korean Chemical Society Comparing equilibrium structures of the Amyloid-β (1-42) dimers and assembly properties in vitro

Submission Date :
8 / 19 / 2021 , 14 : 24 : 31
Abstract Number :
Presenting Type:
Oral Presentation
Presenting Area :
Analytical Chemistry - Oral Presentation of Young Analytical Chemists II
Authors :
Dongjoon Im, MyungKook Son, Chae Ri Park, Sooyeon Chae, Hugh I. Kim*
Department of Chemistry, Korea University, Korea
Assigned Code :
ANAL2.O-18 Assigend Code Guideline
Presenting Time :
FRI, 10 : 42
Senile plaque of Amyloid-β (1-42) is well-known pathological hallmark in Alzheimer’s disease. High aggregation propensity is a major characteristic of Amyloid-β (1-42). In the previous study, we investigated equilibrium ensembles of Amyloid-β (1-42) on the basis of 19.2 μs replica exchange molecular dynamics simulations (400 ns per replica). From this simulation results, we confirmed that hydrophobic interaction plays a pivotal role in the self-assembly process of Amyloid-β (1-42) and contacts between side chains occur frequently in the specific domain. We also observed that substitution of the hydrophobic core residues into hydrophilic amino acid decelerates its fibrillation process. Herein, we obtained equilibrium ensembles of mutant peptide homo dimer and hetero dimer with wild type. To further investigation of inter-molecular states, we performed Markov State Model analysis. The free energy landscape of mutant peptide has multiple local minima whereas the wild type had only one global minimum state. Combined with mass spectrometry analysis, we can understand the underlying mechanisms in kinetical delay of the self-assembly process of Amyloid-β (1-42) with its point mutant.