In silico exploration of PD-L1 binding compounds: Structure-based virtual screening, molecular docking, and MD simulation

Programmed death-ligand 1 (PD-L1), a transmembrane protein, is associated with the regulation of immune system. It frequently has overexpression in various cancers, allowing tumor cells to avoid immune detection. PD-L1 inhibition has risen as a potential strategy in the field of therapeutic immunology for cancer. In the current study, structure-based virtual screening of drug libraries was conducted and then the screened hits were docked to the active residues of PD-L1 to select the optimal binding poses. The top ten compounds with binding affinities ranging from -10.734 to -10.398 kcal/mol were selected for further analysis. The ADMET analysis of selected compounds showed the compounds meet the criteria of ADMET properties. Further, the conformational changes and binding stability of the top two compounds was analyzed by conducting 200 ns simulation and it was observed that the hits did not exert conformational changes to the protein structure. All the results suggest that the chosen hits can be considered as lead compounds for the inhibition of biological activity of PD-L1 in in vitro studies.

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Publication Details

Journal
PLoS ONE
Published
2024-08-09
DOI
https://doi.org/10.1371/journal.pone.0306804
Citations
6
Primary Topic
Computational Drug Discovery Methods
Type
article
Field-Weighted Citation Impact
2.17

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article

In silico exploration of PD-L1 binding compounds: Structure-based virtual screening, molecular docking, and MD simulation

Ashaimaa Y. Moussa, Abdullah R. Alanzi, Ramzi A. Mothana, Imran Ali et al.
6 citations
PLoS ONE
Computational Drug Discovery Methods
2.17
article

In silico exploration of PD-L1 binding compounds: Structure-based virtual screening, molecular docking, and MD simulation

Ashaimaa Y. Moussa, Abdullah R. Alanzi, Ramzi A. Mothana, Imran Ali, Mudassar Abbas
article en
6 citations

Abstract

Programmed death-ligand 1 (PD-L1), a transmembrane protein, is associated with the regulation of immune system. It frequently has overexpression in various cancers, allowing tumor cells to avoid immune detection. PD-L1 inhibition has risen as a potential strategy in the field of therapeutic immunology for cancer. In the current study, structure-based virtual screening of drug libraries was conducted and then the screened hits were docked to the active residues of PD-L1 to select the optimal binding poses. The top ten compounds with binding affinities ranging from -10.734 to -10.398 kcal/mol were selected for further analysis. The ADMET analysis of selected compounds showed the compounds meet the criteria of ADMET properties. Further, the conformational changes and binding stability of the top two compounds was analyzed by conducting 200 ns simulation and it was observed that the hits did not exert conformational changes to the protein structure. All the results suggest that the chosen hits can be considered as lead compounds for the inhibition of biological activity of PD-L1 in in vitro studies.

PLoS ONEVol. 19(8)
Ain Shams University (EG), Gulf University for Science & Technology (KW), King Saud University (SA), Henan University of Technology (CN)
King Saud University
Good health and well-being
Openalex Percentile: Top 11%
Computational Drug Discovery Methods
2.17
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In silico exploration of PD-L1 binding compounds: Structure-based virtual screening, molecular docking, and MD simulation — Ashaimaa Y. Moussa, Abdullah R. Alanzi, et al. · PLoS ONE (2024) | TGRS Research Map | TGRS