低聚物
辣根过氧化物酶
两亲性
单体
化学
碱性磷酸酶
酶
生物化学
肽
过氧化物酶
生物物理学
淀粉样蛋白(真菌学)
生物
有机化学
无机化学
共聚物
聚合物
作者
Ling Mo,Jiang Chen,Congjie Cai,Youguang Guo,Ling‐Hui Zeng,Song Li,Jun Tan
标识
DOI:10.1021/acschemneuro.3c00391
摘要
Recent studies have found that β-amyloid (Aβ) oligomers may play much more important roles than amyloid plaques in the pathogenesis of Alzheimer’s disease (AD). However, due to the complexity of Aβ, studying the structural basis of Aβ oligomer toxicity is challenging. Here, we assessed the amphiphilic property and β-hairpin structure of Aβ monomer. The potential impacts of Aβ oligomers and three sequence-modifying peptides on the enzyme activities of horseradish peroxidase (HRP) and alkaline phosphatase (ALP) were further evaluated. We demonstrated that Aβ oligomer possesses the ability to alter the activity of two enzymes. Moreover, modifications on the hydrophobic region and β-turn structure of Aβ monomer significantly alter its impacts on the enzyme activities. In addition, these modifications also change the bonding modes of Aβ monomers or oligomers binding to HRP, as assessed by molecular docking. All of these findings provide direct experimental evidence to reveal the critical roles of the amphiphilic property and β-sheet structure of Aβ monomer in its impacts on protein activity.
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