BACKGROUNDWe　synthesised　a　novel　sericin　peptide　(SP-GI)　with　-d-glucosidase　inhibitory　activity,　which　has　a　sequence　of　SEDSSEVDIDLGN.　The　kinetics　of　its　peptide-induced　inhibition　on　-d-glucosidase　activity　and　its　interaction　mechanism　merging　with　molecular　docking　were　both　investigated.　RESULTSSP-GI　exhibited　significant　inhibitory　activity　with　an　IC50　of　2.90.1　mu　mol　L-1　and　this　inhibition　was　reversible　and　non-competitive　with　a　K-i　value　of　1.0　+/-　0.1　mu　mol　L-1.　An　interaction　study　with　SP-GI　revealed　it　bound　to　-d-glucosidase　at　a　single　binding　site,　resulting　in　alterations　in　-d-glucosidase　secondary　structure.　This　led　to　quenching　of　intrinsic　-d-glucosidase　fluorescence　by　a　static　quenching　mechanism.　Molecular　docking　results　showed　that　the　SP-GI　binding　site　on　-d-glucosidase　differed　from　acarbose,　with　hydrogen　bonding　and　van　der　Waals　forces　being　the　main　binding　drivers.　CONCLUSIONThese　findings　suggest　the　potential　use　for　SP-GI　or　other　natural　sericin　peptides　as　dietary　supplements　for　the　treatment　of　type　2　diabetes.　(c)　2017　Society　of　Chemical　Industry