Molecular docking study on the interaction of TGF-β receptor 1 and AcSDKP

ObjectiveTo investigate the interaction between TGF-β receptor 1 and (N-Acetyl-Ser-Asp-Lys-Pro) AcSDKP through molecular docking. MethodsThe structures of AcSDKP and its mutations were designed and modeled using Sybyl-X2.1. Molecular docking with Surflex was adopted to elucidate the binding of AcSDKP and its mutations to TGF-β receptor 1. ResultsAcSDKP could stably interact with TGF-β receptor 1, where twelve hydrogen bonds were formed. AcSDKP also increased the binding affinity to TGF-β receptor 1 after mutation of its second residue from aspartic acid (D) to tryptophan (W). However, other mutations on positions of second or third residues decreased binding affinities. ConclusionsAcSDKP is an anti-TGF-β/Smad peptide and can specifically inhibit TGF-β receptor 1. Molecular docking studies suggest that AcSDKP or AcSWDP has stronger binding interactions with TGF-β receptor 1, which are dominated by several hydrogen bonds.