Bodee Nutho

บดี หนูโท

Instructor
+662-201-5651
+662-354-7157
bodee.nut@mahidol.ac.th
Education
  • B.Sc. (Biochemistry, First-Class Honour) Chulalongkorn University, Thailand
  • M.Sc. (Pharmacology) Mahidol University, Thailand
  • Ph.D. (Biotechnology) Chulalongkorn University, Thailand
Current Research
  • Computer-aided drug design and discovery
  • Molecular dynamics simulation of biomolecules
  • Computational enzymology: modelling biocatalyst
Publications
  • Nutho B, Pengthaisong S, Tankrathok A, Lee VS, Cairns JRK, Rungrotmongkol T, et al. Structural basis of specific glucoimidazole and mannoimidazole binding by Os3BGlu7. Biomolecules. 2020;10(6):1-19.
  • Nutho B, Mahalapbutr P, Hengphasatporn K, Pattaranggoon NC, Simanon N, Shigeta Y, et al. Why are lopinavir and ritonavir effective against the newly emerged coronavirus 2019? Atomistic insights into the inhibitory mechanisms. Biochemistry. 2020;59(18):1769-79.
  • Petsri K, Yokoya M, Tungsukruthai S, Rungrotmongkol T, Nutho B, Vinayanuwattikun C, et al. Structure–activity relationships and molecular docking analysis of Mcl-1 targeting renieramycin T analogues in patient-derived lung cancer cells. Cancers. 2020;12(4).
  • Hotarat W, Nutho B, Wolschann P, Wolschann P, Rungrotmongkol T, Rungrotmongkol T, et al. Delivery of alpha-mangostin using cyclodextrins through a biological membrane: Molecular dynamics simulation. Molecules. 2020;25(11).
  • Nutho B, Rungrotmongkol T. Binding recognition of substrates in NS2B/NS3 serine protease of Zika virus revealed by molecular dynamics simulations. J Mol Graph Model. 2019;92:227-35.
  • Nutho B, Mulholland AJ, Rungrotmongkol T. The reaction mechanism of Zika virus NS2B/NS3 serine protease inhibition by dipeptidyl aldehyde: A QM/MM study. Phys Chem Chem Phys. 2019;21(27):14945-56.
  • Nutho B, Mulholland AJ, Rungrotmongkol T. Quantum Mechanics/Molecular Mechanics (QM/MM) Calculations Support a Concerted Reaction Mechanism for the Zika Virus NS2B/NS3 Serine Protease with Its Substrate. J Phys Chem B. 2019;123(13):2889-903.
  • Kammarabutr J, Mahalapbutr P, Nutho B, Kungwan N, Rungrotmongkol T. Low susceptibility of asunaprevir towards R155K and D168A point mutations in HCV NS3/4A protease: A molecular dynamics simulation. J Mol Graph Model. 2019;89:122-30.
  • Boonma T, Nutho B, Rungrotmongkol T, Nunthaboot N. Understanding of the drug resistance mechanism of hepatitis C virus NS3/4A to paritaprevir due to D168N/Y mutations: A molecular dynamics simulation perspective. Comput Biol Chem. 2019;83.
  • Panman W, Nutho B, Chamni S, Dokmaisrijan S, Kungwan N, Rungrotmongkol T. Computational screening of fatty acid synthase inhibitors against thioesterase domain. J Biomol Struct Dyn. 2018;36(15):4114-25.
  • Mahalapbutr P, Nutho B, Wolschann P, Chavasiri W, Kungwan N, Rungrotmongkol T. Molecular insights into inclusion complexes of mansonone E and H enantiomers with various β-cyclodextrins. J Mol Graph Model. 2018;79:72-80.
  • Wongpituk P, Nutho B, Panman W, Kungwan N, Wolschann P, Rungrotmongkol T, et al. Structural dynamics and binding free energy of neral-cyclodextrins inclusion complexes: Molecular dynamics simulation. Mol Simul. 2017;43(13-16):1356-63.
  • Nutho B, Nunthaboot N, Wolschann P, Kungwan N, Rungrotmongkol T. Metadynamics supports molecular dynamics simulation-based binding affinities of eucalyptol and beta-cyclodextrin inclusion complexes. RSC Adv. 2017;7(80):50899-911.
  • Nutho B, Meeprasert A, Chulapa M, Kungwan N, Rungrotmongkol T. Screening of hepatitis C NS5B polymerase inhibitors containing benzothiadiazine core: a steered molecular dynamics. J Biomol Struct Dyn. 2017;35(8):1743-57.
  • Jetsadawisut W, Nutho B, Meeprasert A, Rungrotmongkol T, Kungwan N, Wolschann P, et al. Susceptibility of inhibitors against 3C protease of coxsackievirus A16 and enterovirus A71 causing hand, foot and mouth disease: A molecular dynamics study. Biophys Chem. 2016;219:9-16.
  • Nutho B, Khuntawee W, Rungnim C, Pongsawasdi P, Wolschann P, Karpfen A, et al. Binding mode and free energy prediction of fisetin/β-cyclodextrin inclusion complexes. Beilstein J Org Chem. 2014;10:2789-99.