Understanding the molecular basis for enhanced glutenase activity of actinidin

Management of gluten intolerance is currently possible only by consumption of gluten free diet(GFD) for a lifetime. The scientific community has been searching for alternatives to GFD, like inclusion of natural proteases with meals or pre-treatment of gluten containing foods with glutenases. Actinidin from kiwifruit has shown considerable promise in digesting immunogenic gliadin peptides as compared to other plant derived cysteine proteases. Through this article, we have attempted to understand the structural basis for elevated protease action of actinidin against gliadin peptides by using an in silico approach. Docking experiments reveal key differences between the binding of gliadin peptide to actinidin and papain, which may be responsible for their differential digestive action. Sequence comparison of different plant cysteine proteases highlights amino acid residues surrounding the active site pocket of actinidin that are unique to this molecule and hence likely to contribute to its digestive properties. Graphical summary O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=64 SRC="FIGDIR/small/542047v1_ufig1.gif" ALT="Figure 1"> View larger version (25K): org.highwire.dtl.DTLVardef@4fcd61org.highwire.dtl.DTLVardef@134c371org.highwire.dtl.DTLVardef@10b5d78org.highwire.dtl.DTLVardef@1257d19_HPS_FORMAT_FIGEXP M_FIG C_FIG