Beking Kris, Hao Xiaolei, Basak Sarmistha, Basak Ajoy
Regional Protein Chemistry Center, Diseases of Aging Program, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, ON. K1Y 4E9, Canada.
Protein Pept Lett. 2005 Feb;12(2):197-202. doi: 10.2174/0929866053005845.
The study explores in vitro by circular dichroism and mass spectrometry the effects of pH, Cu+2 ions and sheet-breakers on the secondary structures and self-aggregation of beta-amyloid peptides [Abeta43, Abeta42 and Abeta40] of Alzheimer's disease. Within pH 5.4-7.3, more sheet structures and aggregates containing up to 11 peptide units were observed. Cu+2 ions led to oxidative degradation or aggregation depending on its concentration and time of incubation. beta-sheet breakers can reverse the self-aggregation process, suggesting their potential therapeutic use.
该研究通过圆二色光谱法和质谱法在体外探究了pH值、铜离子(Cu²⁺)和β-折叠破坏剂对阿尔茨海默病β-淀粉样肽[Abeta43、Abeta42和Abeta40]二级结构和自聚集的影响。在pH 5.4至7.3范围内,观察到更多的β-折叠结构以及含有多达11个肽单元的聚集体。铜离子(Cu²⁺)根据其浓度和孵育时间导致氧化降解或聚集。β-折叠破坏剂可以逆转自聚集过程,表明它们具有潜在的治疗用途。