Institute of Pathophysiology, Faculty of Medicine, Zaloška 4, SI-1000 Ljubljana, Slovenia.
Molecules. 2018 Jan 30;23(2):283. doi: 10.3390/molecules23020283.
Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and integrated by proteostasis. The frequency of protein misfolding disorders in the human population, e.g., in Alzheimer's disease (AD), is increasing due to the aging population. AD treatment options are limited to symptomatic interventions that at best slow-down disease progression. The key biochemical change in AD is the excessive accumulation of per-se non-toxic and soluble amyloid peptides (Aβ(1-37/44), in the intracellular and extracellular space, that alters proteostasis and triggers Aβ modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble Aβ peptides, Aβ dimers and Aβ oligomers. The toxic intermediate Aβ products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic Aβ oligomerization, Aβ aggregation into fibrils, or stabilize Aβ peptides in non-toxic oligomers, and discusses their potential for AD treatment.
蛋白质的细胞内合成、折叠、运输和降解受到蛋白质稳态的控制和整合。由于人口老龄化,人类蛋白质错误折叠疾病(例如阿尔茨海默病(AD))的发病率正在增加。AD 的治疗选择仅限于对症干预,最多只能减缓疾病进展。AD 的关键生化变化是细胞内和细胞外空间中过量积累原本无毒且可溶的淀粉样肽(Aβ(1-37/44)),这会改变蛋白质稳态并引发 Aβ 修饰(例如,通过活性氧(ROS))成有毒中间体、错误折叠的可溶性 Aβ 肽、Aβ 二聚体和 Aβ 寡聚体。有毒中间体 Aβ 产物聚集成毒性逐渐降低且可溶性降低的原纤维、纤维和老年斑。本综述重点介绍了抑制有毒 Aβ 寡聚化、Aβ 纤维形成或稳定无毒 Aβ 寡聚物的肽,并讨论了它们在 AD 治疗中的潜力。