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Front Cover: MPI8 is Potent against SARS‐CoV‐2 by Inhibiting Dually and Selectively the SARS‐CoV‐2 Main Protease and the Host Cathepsin L (ChemMedChem 1/2022)
Author(s) -
Ma Xinyu R.,
Alugubelli Yugendar R.,
Ma Yuying,
Vatansever Erol C.,
Scott Danielle A.,
Qiao Yuchen,
Yu Ge,
Xu Shiqing,
Liu Wenshe Ray
Publication year - 2022
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.202100769
Subject(s) - protease , cathepsin l , chemistry , covid-19 , front cover , potency , virology , cathepsin b , cathepsin , protease inhibitor (pharmacology) , in vitro , virus , cathepsin d , microbiology and biotechnology , enzyme , biochemistry , cover (algebra) , biology , medicine , viral load , mechanical engineering , disease , pathology , antiretroviral therapy , infectious disease (medical specialty) , engineering
The Front Cover shows that MPI8, a SARS‐CoV‐2 main protease inhibitor, dually inhibits human cathepsin L to prevent the SARS‐CoV‐2 RNA genome from leaving the endosome. MPI8 is a reversible covalent inhibitor of the SARS‐CoV‐2 main protease that displays high potency in inhibiting the virus in vitro . It also selectively inhibits human cathepsin L over other tested human cathepsins. Cover design by Dr. Xinyu Ma. More information can be found in the Full Paper by Xinyu R. Ma, Shiqing Xu, Wenshe Ray Liu et al.