TY - JOUR
T1 - Potential novel inhibitors against emerging zoonotic pathogen Nipah virus
T2 - a virtual screening and molecular dynamics approach
AU - Ropón-Palacios, Georcki
AU - Chenet-Zuta, Manuel E.
AU - Olivos-Ramirez, Gustavo E.
AU - Otazu, Kewin
AU - Acurio-Saavedra, Jorge
AU - Camps, Ihosvany
N1 - Publisher Copyright:
© 2019, © 2019 Informa UK Limited, trading as Taylor & Francis Group.
PY - 2020/7/23
Y1 - 2020/7/23
N2 - Nipah virus is a pathogen considered highly infectious, and its lethality can cause between 40% and 70% of deaths in those infected. At present, no effective treatment is available which results in an imperative need to explore new approaches to the search for drugs. Through virtual screening techniques, docking and molecular dynamics, 183 ligands were evaluated against the Nipah virus glycoprotein (NiV-G), involved throughout the process of virus entry to the host cell, resulting in a good target for blocking the infection. Of the 183 drugs computationally screened, three of them (MMV020537, MMV688888 and MMV019838) were found to be potential inhibitors of NiV-G. Their calculated dissociation constants were 0.03 nM, 2.18 nM and 31.61 nM, respectively. Molecular dynamics studies confirm their stability binding modes in the active site of the protein. These potential inhibitors can be used later as leads for the development of new drugs that allow effective treatment of the disease. Communicated by Ramaswamy H. Sarma.
AB - Nipah virus is a pathogen considered highly infectious, and its lethality can cause between 40% and 70% of deaths in those infected. At present, no effective treatment is available which results in an imperative need to explore new approaches to the search for drugs. Through virtual screening techniques, docking and molecular dynamics, 183 ligands were evaluated against the Nipah virus glycoprotein (NiV-G), involved throughout the process of virus entry to the host cell, resulting in a good target for blocking the infection. Of the 183 drugs computationally screened, three of them (MMV020537, MMV688888 and MMV019838) were found to be potential inhibitors of NiV-G. Their calculated dissociation constants were 0.03 nM, 2.18 nM and 31.61 nM, respectively. Molecular dynamics studies confirm their stability binding modes in the active site of the protein. These potential inhibitors can be used later as leads for the development of new drugs that allow effective treatment of the disease. Communicated by Ramaswamy H. Sarma.
KW - molecular docking
KW - molecular dynamics
KW - Nipah virus
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U2 - 10.1080/07391102.2019.1655480
DO - 10.1080/07391102.2019.1655480
M3 - Article
C2 - 31411538
VL - 38
SP - 3225
EP - 3234
JO - Journal of Biomolecular Structure and Dynamics
JF - Journal of Biomolecular Structure and Dynamics
SN - 0739-1102
IS - 11
ER -