Department of Chemistry, Bar-Ilan University, Ramat-Gan 5290002, Israel.
Chem Commun (Camb). 2018 Jun 8;54(47):5980-5983. doi: 10.1039/c8cc01233d.
Aggregation and accumulation of amyloid β and tau proteins to plaques and neurofibrillary tangles are the key pathogenic events in Alzheimer's disease. Here, we studied the capability of the cyclic d,l-α-peptide CP-2 as a conformational inhibitor of different amyloids to cross-interact with tau-derived AcPHF6 peptide and inhibit its aggregation, membrane perturbation and toxicity.
淀粉样 β 和 tau 蛋白的聚集和积累形成斑块和神经原纤维缠结是阿尔茨海默病的关键致病事件。在这里,我们研究了环状 d,l-α-肽 CP-2 作为不同淀粉样蛋白构象抑制剂的能力,以与 tau 衍生的 AcPHF6 肽交叉相互作用并抑制其聚集、膜扰动和毒性。