ArticlePloS one2024
In silico exploration of PD-L1 binding compounds: Structure-based virtual screening, molecular docking, and MD simulation.
Article in PloS one, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- In silico screen identifies Pranidipine as a potential inhibitor of the PD-1/PD-L1 immune checkpoint.Scientific reports · 2026Article
- Computational identification and evaluation of novel PD-L1 inhibitors for cancer immunotherapy.Scientific reports · 2025Article
- Role of Saponins fromMolecules (Basel, Switzerland) · 2025Article
- Article
- Exploring the Potential of Peptides Derived from the Coelomic Fluid ofF1000Research · 2025Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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