Fig. 8

Molecular docking interactions of TBEP with core cancer-related proteins. (A):TBEP binds SRC via five hydrogen bonds (SER94, ASP99, SER101; 2.7–3.4 Å) and hydrophobic interactions with THR103 and GLU128. (B): TBEP forms four hydrogen bonds (GLN203, HIS207, TYR385, TRP387; 2.28–3.5 Å) and hydrophobic contacts with HIS237, TRP340, plus a salt bridge with ARG341 in CASP3. (C): TBEP interacts hydrophobically with seven residues (VAL64, LEU67, PHE71, VAL164, LEU167, PHE171, ILE175) in ERBB2, without hydrogen bonds or salt bridges. (D): In PTGS2, TBEP establishes five hydrogen bonds (GLN203, HIS388, HIS207, TYR385, TRP387; 3.1–3.2 Å), hydrophobic interactions with four residues, and two salt bridges (HIS207, HIS388). (E): TBEP forms three hydrogen bonds (ARG116, GLU104; 3.2–3.4 Å), hydrophobic contacts with three residues, and a salt bridge with HIS99 in MTOR. (F): TBEP binds ESR1 through one hydrogen bond (GLY390; 2.9 Å) and hydrophobic interactions with seven residues. (G): In BCL2, TBEP establishes four hydrogen bonds (LYS53, LYS101, GLU49; 2.2–3.6 Å), hydrophobic contacts with four residues, and a salt bridge with ARG362. (H): TBEP engages FOS via five hydrogen bonds (LYS69, LEU7; 2.1–3.0 Å), a hydrophobic contact with TYR65, and a salt bridge with LYS69. (I): TBEP interacts with MAPK14 through two hydrogen bonds (ASP88, ARG23; 3.1–3.3 Å), hydrophobic interactions with three residues, and a salt bridge with LYS69. (J): TBEP forms six hydrogen bonds (ARG362, SER385, ASN336; 3.0–3.3 Å), hydrophobic contacts with seven residues, and a salt bridge with ARG362 in ABL1. K: In MAPK8, TBEP forms five hydrogen bonds (THR21, GLY35, ALA36, ASN156, SER155, LYS153; 3.2–6.3 Å) and hydrophobic interactions with three residues. L: TBEP binds CDK1 via three hydrogen bonds (GLN132, TYR15; 3.2–3.4 Å) and hydrophobic interactions with seven residues.