TY - JOUR
T1 - Interdiction of Protein Folding for Therapeutic Drug Development in SARS CoV-2
AU - Bergasa-Caceres, Fernando
AU - Rabitz, Herschel A.
N1 - Publisher Copyright:
Copyright © 2020 American Chemical Society.
PY - 2020/9/24
Y1 - 2020/9/24
N2 - In this article, we predict the folding initiation events of the ribose phosphatase domain of protein Nsp3 and the receptor binding domain of the spike protein from the severe acute respiratory syndrome (SARS) coronavirus-2. The calculations employ the sequential collapse model and the crystal structures to identify the segments involved in the initial contact formation events of both viral proteins. The initial contact locations may provide good targets for therapeutic drug development. The proposed strategy is based on a drug binding to the contact location, thereby aiming to prevent protein folding. Peptides are suggested as a natural choice for such protein folding interdiction drugs.
AB - In this article, we predict the folding initiation events of the ribose phosphatase domain of protein Nsp3 and the receptor binding domain of the spike protein from the severe acute respiratory syndrome (SARS) coronavirus-2. The calculations employ the sequential collapse model and the crystal structures to identify the segments involved in the initial contact formation events of both viral proteins. The initial contact locations may provide good targets for therapeutic drug development. The proposed strategy is based on a drug binding to the contact location, thereby aiming to prevent protein folding. Peptides are suggested as a natural choice for such protein folding interdiction drugs.
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U2 - 10.1021/acs.jpcb.0c03716
DO - 10.1021/acs.jpcb.0c03716
M3 - Article
C2 - 32790379
AN - SCOPUS:85091600285
SN - 1520-6106
VL - 124
SP - 8201
EP - 8208
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 38
ER -