Molecular docking of HSV-1 for identification of sulfolipid (SQDG) targeted protein

Abstract

The binding of non-ionic (L1) and ionic (1.2) forms of sulfo-quinovosyl-diacyf-glycerol (SQDG) structure, in three target protein structures of Herpes Simplex Virus Type 1 (HSV-1), i.e. HSV-1 DNA polymerase (HSV-1 DNAPol); Glycoprotein D (gD); and Thymidine kinase (TK),were investigated using GOLD programe.Results showed that both L1 and L2 posed the high fitness score with HSV-1 DNAPol chain B (46.49 and 44.49, respectively) Amino acid containing positively charged sidechain, i.e. arginine (Arg), was found to be important in the binding to hydrophillic region of sulfonyl group, while amino acid containing hydrophobic sidechain revealed the interaction to hydrophobic region, fatty acid chains, of the sulfolipid