One major cause of Alzheimer’s disease(AD) is evidently due to the aggregation and deposition of amyloidβ peptides(Aβ) in the brain tissue of the patient. Preventing misfolding and self-aggregation of Aβ protein c...One major cause of Alzheimer’s disease(AD) is evidently due to the aggregation and deposition of amyloidβ peptides(Aβ) in the brain tissue of the patient. Preventing misfolding and self-aggregation of Aβ protein can reduce the formation of highly toxic polymer, which is important for the treatment of AD. Among them, the α-helix consisting of42 residues(Aβ42) is the main component of senile plaques in AD. In this paper, 500 ns accelerated molecular dynamics are performed at different temperatures(300 K, 350 K, 400 K, 450 K) to study of the effect of temperature-induced conformation changes of Aβ42 protein during the unfolding process respectively.展开更多
基金Supported by the National Natural Science Foundation of China under Grant Nos.11574184,11774207the Natural Science Foundation of Shandong Province under Grant No.ZR2016JL003Primary Research&Development Plan of Shandong Province under Grant No.2017GSF18108
文摘One major cause of Alzheimer’s disease(AD) is evidently due to the aggregation and deposition of amyloidβ peptides(Aβ) in the brain tissue of the patient. Preventing misfolding and self-aggregation of Aβ protein can reduce the formation of highly toxic polymer, which is important for the treatment of AD. Among them, the α-helix consisting of42 residues(Aβ42) is the main component of senile plaques in AD. In this paper, 500 ns accelerated molecular dynamics are performed at different temperatures(300 K, 350 K, 400 K, 450 K) to study of the effect of temperature-induced conformation changes of Aβ42 protein during the unfolding process respectively.
