Journal
MOLECULES
Volume 23, Issue 2, Pages -Publisher
MDPI
DOI: 10.3390/molecules23020283
Keywords
aggregation; Alzheimer's disease; amyloid beta oligomers; amyloid beta peptide; amyloid beta plaques; insulin; neurofibrillary tangles; tau protein; peptides; peptide therapy
Funding
- ARRS [P3-0171]
Ask authors/readers for more resources
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 (A beta (1-37/44), in the intracellular and extracellular space, that alters proteostasis and triggers A beta modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble A beta peptides, A beta dimers and A beta oligomers. The toxic intermediate A beta products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic A beta oligomerization, A beta aggregation into fibrils, or stabilize A beta peptides in non-toxic oligomers, and discusses their potential for AD treatment.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available