TY - JOUR ID - 4412 TI - Inhibitory effect of corcin on aggregation of 1N/4R human tau protein in vitro JO - Iranian Journal of Basic Medical Sciences JA - IJBMS LA - en SN - 2008-3866 AU - Mohammadi Karakani, Ali AU - Riazi, Gholamhossein AU - Ghaffari, Seyed Mahmood AU - Ahmadian, Shahin AU - Mokhtari, Farzad AU - Jalili Firuzi, Mahshad AU - Bathaie, Seyedeh Zahra AD - Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran AD - Department of Clinical Biochemistry, Tarbiat Modares University, Tehran, Iran Y1 - 2015 PY - 2015 VL - 18 IS - 5 SP - 485 EP - 492 KW - Alzheimer's disease KW - Anti-aggregation KW - Crocin KW - Tau protein DO - 10.22038/ijbms.2015.4412 N2 - Objective(s):Alzheimer's disease (AD) is the most common age-related neurodegenerative disorder. One of the hallmarks of AD is an abnormal accumulation of fibril forms of tau protein which is known as a microtubule associated protein. In this regard, inhibition of tau aggregation has been documented to be a potent therapeutic approach in AD and tauopathies. Unfortunately, the available synthetic drugs have modest beneficial efficacy with several side effects. Therefore, pipeline drugs from natural sources with anti-aggregation properties can be useful in the prevention and treatment of AD. Among medicinal plants, saffron (Crocus sativus, L.), as a traditional herbal medicine has different pharmacological properties and can be used as treatment for several nervous system impairment including depression and dementia. Crocin as a major constituent of saffron is the glycosylated form of crocetin. Materials and Methods:  In this study, we investigated the inhibitory effect of crocin on aggregation of recombinant human tau protein 1N/4R isoform using biochemical methods and cell culture. Results:  Results revealed that tau protein under the fibrillation condition and in the presence of crocin had enough stability with low tendency for aggregation. Crocin inhibited tau aggregation with IC50 of 100 µg/ml.  Furthermore, transmission electron microscopy images confirmed that crocin could suppress the formation of tau protein filaments. Conclusion: Inhibitory effect of crocin could be related to its interference with nucleation phase that led to increases in monomer species of tau protein. Based on our results, crocin is recommended as a proper candidate to be used in AD treatment. UR - https://ijbms.mums.ac.ir/article_4412.html L1 - https://ijbms.mums.ac.ir/article_4412_731abb48103216aac31515fb5607cb7f.pdf ER -