NATURE-BASED TAU PROTEIN AGGREGATION INHIBITORS AS VALUABLE THERAPEUTIC COMPONENTS FOR TREATING ALZHEIMER’S DISEASES
Authors: Kishor R. Danao , ABOLI S. MALOKAR, DEBARSHI KAR MAHAPATRA AND UJWALA N. MAHAJAN

ABSTRACT
Background: Alzheimer’s disease is progressive degenerative disorders of the brain that begins with memory impairment and eventually progresses to dementia, physical impairment, and death. Tau protein belongs to the family of microtubule association protein. They are mainly present in neurons, where they do important work; they assemble tubulin monomers into the microtubule networks. Molecular analysis depicted that abnormal phosphorylation might be an important event in the pathogenesis where tau is the remarkable marker of the neurodegenerative process. Methodology: This review article was written after collecting a huge amount of latest literature on Tau protein inhibitors from varied pharmaceutical databases like ScienceDirect, PubMed, Google Scholar, etc. by using specific keywords. The collected data was appropriately classified and justified. Results: The article moreover focuses on various natural products [Plant-derived (paclitaxel, curcumin, oleocanthal, diallyl disulfide, emodin, S-allyl cysteine, cinnamaldehyde, tanshinoneIIA,myricanone, and rosmarinic acid); Microbes-derived (adriamycin, daunorubicin, geldanamycin, rubellin-B, rubellin-D, rubellin-E, minocycline, epithilone-D, and fulvic acid); and Marine macroorganism-derived (peloruside-A, manzamine-A, palinurin, and hymenialdisine)] that acts as tau-protein aggregation inhibitors. Conclusion: This fascinating literature concluded that the low molecular-weight natural inhibitors will positively provide research information or serve as a futuristic lead to enthusiastic medicinal chemists and curious pharmacologists in managing Alzheimer’s disease by opening application avenues via pharmacotherapeutic approach. Keywords: Alzheimer's disease, Tau protein, Inhibitors, Natural, Microbes, Marines
Publication date: 15/12/2021
    https://ijbpas.com/pdf/2021/December/MS_IJBPAS_2021_DEC_SPCL_1038.pdf
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https://doi.org/10.31032/IJBPAS/2021/10.12.1038