In the present study, the molecular dynamic was cross-correlated with the docking design for the three-drug delivery platforms. The milestones were to understand the interaction between the SAR7334-functionalised nanoparticles (SAR-NPs) and the Transient Receptor Potential Cation Channel Subfamily C member 6 (TPRC6). In addition, we compared results with the other two ligands of TRPC6 (SAR-DBCO and SAR-PEG4-DBCO). Based on a virtual screening we found that SAR-DBCO has a higher binding affinity among the tested inhibitors (-10.7 kcal/mol). SAR7334 showed a slightly lower binding affinity (-8.1 kcal/mol) and display similar key interactions with SAR-DBCO some key interactions with amino acid residues of the receptor. In particular, the hydrogen-bond analysis indicated that both SAR-DBCO and SAR7334 form an H-bond with a glutamine residue (GLN624) of TRPC6, and this interaction is part of hydrogen bond networks that play a positive role in strengthening the binding effect between the receptor and its ligands. The structural stability and validation of the obtained docking scores were validated and analyzed by the frame of Molecular dynamics simulations.

Docking studies and molecular dynamics simulations of SAR7334-functionalised nanoparticles (SAR-NPs) and the transient receptor potential cation channel subfamily C member 6 (TPRC6)

ACS Fall 2021

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Docking studies and molecular dynamics simulations of SAR7334-functionalised nanoparticles (SAR-NPs) and the transient receptor potential cation channel subfamily C member 6 (TPRC6) </i>