National Academy of Agricultural Sciences (NAAS)
|
PRINT ISSN : 2319-7692
Online ISSN : 2319-7706 Issues : 12 per year Publisher : Excellent Publishers Email : editorijcmas@gmail.com / submit@ijcmas.com Editor-in-chief: Dr.M.Prakash Index Copernicus ICV 2018: 95.39 NAAS RATING 2020: 5.38 |
Prion diseases is a neurodegenerative disorder that effects the brain and nervous system. This disease alters the normal functioning of nervous system and have same molecular mechanism and proteins involved both in humans and animals. Prion disease is caused by the deposition of abnormally folded proteins in the brain, that causes changes in memory, behavior, and movement. Prion diseases causes a progressive decline in the brain function due to misfolding of proteins called prion proteins (PrP). Misfolded PrP begins to accumulate and form clumps within the brain, damaging and killing nerve cells. Current research was done to screen and study the neurological drugs against prion disease. To predict potential drug that can be used for drug development and discovery. In this research two prion proteins i.e., PrPLP /Prion Protein 2(PDB ID: 1I4M) and ERI1 Exoribonuclease 3protein (PDB ID: 2XRI) were selected as drug target. These proteins were docked against 20 ligands screened from PubChem database. These 20 ligands were selected based on reference research papers, extensive literature search and these ligands have function in neurological diseases and act as drug. Twenty selected ligands were docked against target protein using CB dock server. Docking result shows that Prion protein 2 shows best interaction with Celastrol with a Vina Score of -8.2 and in ERI1 Exoribonuclease 3 shows best interaction with Celastrol and Amisulpride with a Vina score of -9.7 and -8.8 respectively. This study gives insight into the potential ligand for prion disease and can be used for drug designing process.
Abdelaziz D H, Abdulrahman B A, Gilch S, Schatzl H M. 2019. Autophagy pathways in the treatment of prion diseases. Current opinion in pharmacology, 44:46-52. https://doi.org/10.1016/j.coph.2019.04.013
Amano R, Tsukada S, Kosuge S, Yano S, Ono K, Yoneda M, Taki K. 2021. Case Report: Paraneoplastic Hashimoto's Encephalopathy Associated With Lymphomatosis cerebri With Periodic Synchronous Discharges Resembling Creutzfeldt–Jakob Disease. Frontiers in neurology, 12 :701178. https://doi.org/10.3389/fneur.2021.701178
Ayers J I, Paras N A, Prusiner S B. 2020. Expanding spectrum of prion diseases. Emerging topics in life sciences, 4:155-67. https://doi.org/10.1042/ETLS20200037
Baiardi S, Rossi M, Capellari S, Parchi P. 2019. Recent advances in the histo?molecular pathology of human prion disease. Brain Pathology, 29:278-300. https://doi.org/10.1111/bpa.12695
Blaszczyk M, Ciemny M P, Kolinski A, Kurcinski M, Kmiecik S. 2019. Protein–peptide docking using CABS-dock and contact information. Briefings in bioinformatics, 20:2299-305. https://doi.org/10.1093/bib/bby080
Carroll J A and Chesebro B. 2019. Neuroinflammation, microglia, and cell-association during prion disease. Viruses, 11:65. https://doi.org/10.3390/v11010065
Connor A, Wang H, Appleby B S, Rhoads D D. 2019. Clinical laboratory tests used to aid in diagnosis of human prion disease. Journal of clinical microbiology, 57:e00769-19. https://doi.org/10.1128/JCM.00769-19
Houston F, Andréoletti O. 2019. Animal prion diseases: the risks to human health. Brain pathology.29:248-62.
Hunto S T, Kim H G, Baek K S, Jeong D, Kim E, Kim J H, Cho J Y. 2020. Loratadine, an antihistamine drug, exhibits anti-inflammatory activity through suppression of the NF-kB pathway. Biochemical pharmacology, 177:113949. https://doi.org/10.1016/j.bcp.2020.113949
Jelsma J, Kleinveld H, Rozemuller A, Heyligers I. 2020. Neurology in metal-on-metal hip arthroplasty a case of suspected prosthetic hip-associated cobalt toxicity. Acta Orthopaedica Belgica, 86:1.
Krance S H, Luke R, Shenouda M, Israwi A R, Colpitts S J, Darwish L, Strauss M, Watts J C. 2020. Cellular models for discovering prion disease therapeutics: Progress and challenges. Journal of Neurochemistry, 153:150-172. https://doi.org/10.1111/jnc.14956
Kushwaha R, Sinha A, Makarava N, Molesworth K, Baskakov I V. 2021. Non-cell autonomous astrocyte-mediated neuronal toxicity in prion diseases. Acta Neuropathologica Communications, 9:1-23. https://doi.org/10.1186/s40478-021-01123-8
Lahiri D, Dubey S, Ray B K, Ardila A. 2020. Hallucinatory palinopsia and paroxysmal oscillopsia as initial manifestations of sporadic Creutzfeldt-Jakob disease: A case study. Cortex, 124:188-192. https://doi.org/10.1016/j.cortex.2019.11.017
Li L, Li L, Shang D W, Wen Y G, Ning Y P. 2020. A systematic review and combined meta?analysis of concentration of oral amisulpride. British Journal of Clinical Pharmacology, 86:668-78. https://doi.org/10.1111/bcp.14246
Liberski P P, Gajos A, Sikorska B, Lindenbaum S. 2019. Kuru, the first human prion disease. Viruses, 11:232. https://doi.org/10.3390/v11030232
Liu Y, Grimm M, Dai W T, Hou M C, Xiao Z X, Cao Y. 2020. C B-Dock: a web server for cavity detection-guided protein–ligand blind docking. Acta Pharmacologica Sinica, 41:138-144. https://doi.org/10.1038/s41401-019-0228-6
Minikel E V, Vallabh S M, Orseth M C, Brandel J P, Haïk S, Laplanche J L, Zerr I, Parchi P, Capellari S, Safar J, Kenny J. 2019. Age at onset in genetic prion disease and the design of preventive clinical trials. Neurology, 93:e125-134. https://doi.org/10.1212/WNL.0000000000007745
Minikel E V, Zhao H T, Le J, O’Moore J, Pitstick R, Graffam S, Carlson G A, Kavanaugh M P, Kriz J, Kim J B, Ma J. 2020. Prion protein lowering is a disease-modifying therapy across prion disease stages, strains and endpoints. Nucleic acids research, 48:10615-31. https://doi.org/10.1093/nar/gkaa616
Nazar A B, Adhila Beegam K A, Skinner A, Dastidar D G, Antony E J, Malavika B R, Siddiqui M, Mol R, Elumalai P. 2022. Prophylaxis Through Marine-Derived Bioactive Compounds Toward Neurodegenerative Disorders. In Functional Foods and Therapeutic Strategies for Neurodegenerative Disorders, Springer, Singapore 101-120. https://doi.org/10.1007/978-981-16-6703-9_7
Porter A L, Prusinski C C, Lazar E, Yuh C, Bucelli R C, Appleby B S, Day G S. 2022. Prevalence of Surgical Procedures at Symptomatic Onset of Prion Disease. JAMA Network Open, 5:e221556. https://doi.org/10.1001/jamanetworkopen.2022.1556
Pritzkow S, Morales R, Lyon A, Concha-Marambio L, Urayama A, Soto C. 2018. Efficient prion disease transmission through common environmental materials. Journal of biological chemistry, 293:3363-73. https://doi.org/10.1074/jbc.M117.810747
Rhoads D D, Wrona A, Foutz A, Blevins J, Glisic K, Person M, Maddox R A, Belay E D, Schonberger L B, Tatsuoka C, Cohen M L. 2020. Diagnosis of prion diseases by RT-QuIC results in improved surveillance. Neurology, 95:e1017-26. https://doi.org/10.1212/WNL.0000000000010086
Sigurdson C J, Bartz J C, Glatzel M. 2019. Cellular and molecular mechanisms of prion disease. Annual Review of Pathology: Mechanisms of Disease.14:497-516. https://doi.org/10.1146/annurev-pathmechdis-012418-013109
Singh Y K. 2020/2021. A Review on Protein Misfolding Diseases and therapeutics for preventing Diseases. Journal of Drug Delivery and Therapeutics, 11:221-3. http://dx.doi.org/10.22270/jddt.v11i5.5047
Un H, Ugan RA, Kose D, Bayir Y, Cadirci E, Selli J, Halici Z. 2020. A novel effect of Aprepitant: Protection for cisplatin-induced nephrotoxicity and hepatotoxicity. European journal of pharmacology, 880:173168. https://doi.org/10.1016/j.ejphar.2020.173168
Vallabh S M, Minikel E V, Williams V J, Carlyle B C, McManus A J, Wennick C D, Bolling A, Trombetta B A, Urick D, Nobuhara C K, Gerber J. 2020. Cerebrospinal fluid and plasma biomarkers in individuals at risk for genetic prion disease. BMC medicine, 18; 18(1):140. https://doi.org/10.1186/s12916-020-01608-8
Xu S, Feng Y, He W, Xu W, Xu W, Yang H, Li X. 2021. Celastrol in metabolic diseases: progress and application prospects. Pharmacological research, 167:105572. https://doi.org/10.1016/j.phrs.2021.105572
Zheng Z, Zhang M, Wang Y, Ma R, Guo C, Feng L, Wu J, Yao H, Lin D. 2018. Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease. Scientific reports, 8:1-5. https://doi.org/10.1038/s41598-018-31394-6
Citations |
 |
 |
 |
 |
