Molecular Modeling Studies: Potential Binding of Soy Protein 7S Globulin Subunits to Human LDL Receptor

Abstract

Soybean 7S Globulin subunits have been associated with a decrease in cholesterol both in in vitro and in vivo studies1. One possible mechanism could be binding of the protein or its digested fragments to the LDL receptor. In order to explore the feasibility of this hypothesis, molecular modeling experiments were performed using homology modeling software (MOE, Chemical Computing Group, Inc.) and protein‐protein docking software (FTDock, RPScore & Multidock from Biomolecular Modeling Laboratory, Imperial Cancer Research Fund). In these studies, a homology model was generated for the 7S globulin based on the x‐ray crystal structure of a hydrolase inhibitor from wheat (1T6E.pdb). The LDL receptor binding site was also obtained from the Protein Data Bank (IN7D.pdb). From these docking studies it was observed that the homology model bound to several sites of the extra‐cellular region of the LDL receptor. Possible interactions of 7S Globulin peptide fragments with cyclophilin were modeled and were identified as definite interactions or associations.