Intrinsically　disordered　proteins　(IDPs)　lack　stable　tertiary　structures　under　physiological　conditions,　yet　play　key　roles　in　biological　processes　and　associated　with　human　complex　diseases.　Their　conformational　characteristics　and　high　content　of　charged　residues　make　the　use　of　polarizable　force　fields　an　advantageous　for　simulating　IDPs.　The　Drude2019IDP　polarizable　force　field,　previously　introduced,　has　demonstrated　comprehensive　enhancements　and　improvements　in　dipeptides,　short　peptides,　and　IDPs,　achieving　a　balanced　sampling　between　IDPs　and　structured　proteins.　However,　the　performance　in　simulating　5　dipeptides　was　found　to　be　underestimate.　Therefore,　we　individually　performed　reweighting　and　grid-based　energy　correction　map　(CMAP)　optimization　for　these　5　dipeptides,　resulting　in　the　enhanced　Drude2019IDPC　force　field.　The　performance　of　Drude2019IDPC　was　evaluated　with　5　dipeptides,　5　disordered　short　peptides,　and　a　representative　IDP.　The　results　demonstrated　a　marked　improvement　comparing　with　original　Drude2019IDP.　To　further　substantiate　the　capabilities　of　Drude2019IDPC,　MD　simulation　and　Markov　state　model　(MSM)　were　applied　to　wild　type　and　mutant　for　insulin,　to　elucidate　the　difference　of　conformational　characteristics　and　transition　path.　The　findings　reveal　that　mutation　can　maintain　the　monomorphic　characteristics,　providing　insights　for　engineered　insulin　development.　These　results　indicate　that　Drude2019IDPC　could　be　used　to　reveal　the　structure-function　relationship　for　other　proteins.