Cross-fibrillation of insulin and amyloid β on chiral surfaces: Chirality affects aggregation kinetics and cytotoxicity
作者： Zhi Du , Yijia Guan , Chao Ding , Nan Gao , Jinsong Ren
DOI: 10.1007/S12274-018-1995-Y
关键词:
摘要: Recent clinical and epidemiological research has shown that insulin is associated with the pathological mechanisms of Alzheimer’s disease (AD) can protect against oxidative stress triggered by amyloid-β peptide (Aβ). Herein, we present a systematic study on how cross-fibrillation Aβ influenced surface chirality an interface designed to mimic their aggregation cytomembrane. Intriguingly, strongly affected kinetics, structure, morphology, cellular responses cross-aggregates Aβ. On D-phenylalanine-modified surface, induced co-aggregate into β-sheet-rich fibrils cross-fibrils showed pronounced toxicity. However, L-phenylalanine-modified formed non-toxic amorphous aggregates. Our work indicates influence as well cytotoxicity
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