Highlighted Paper selected by Editor-in-Chief : Modeling Analysis of Potential Target of Dolastatin 16 by Computational Virtual Screening

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  • Liang Ting-Ting
    School of Chemical and Environmental Engineering, Shanghai Institute of Technology Department of Development Technology of Marine Resources, College of Life Sciences, Zhejiang Sci-Tech University
  • Zhao Qi
    Faculty of Health Sciences, University of Macau
  • He Shan
    Li Dak Sum Yip Yio Chin Kenneth Li Marine Biopharmaceutical Research Center, Ningbo University
  • Mu Fang-Zhou
    Pharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison
  • Deng Wei
    School of Chemical and Environmental Engineering, Shanghai Institute of Technology
  • Han Bing-Nan
    Department of Development Technology of Marine Resources, College of Life Sciences, Zhejiang Sci-Tech University

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  • Modeling Analysis of Potential Target of Dolastatin 16 by Computational Virtual Screening

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<p>Dolastatin 16 is a cyclic depsipeptide isolated from the marine invertebrates and cyanobacterium Lyngbya majuscula, however, its bioactivity has been a historical question. In this study, peptidyl–prolyl cis–trans isomerase FKBP1A (FKBP12) was predicted as a potential target of dolastatin 16 via PharmMapper as well as verified using chemical–protein interactome (CPI) and molecular docking. FKBP1A has been previously identified as a target for the natural polyketide FK506 (tacrolimus), an immune suppressor inhibiting the rejection of organ transplantation in clinical use. The comparison study via the reverse pharmacophore screening and molecular docking of dolastatin 16 and FK506 indicated the good consistency of analysis with the computational approach. As the results, the lowest binding energy of dolastatin 16–FKBP1A complex was −7.4 kcal/mol and FK506–FKBP1A complex was −8.7 kcal/mol. The ligand dolastatin 16 formed three hydrogen bonds vs. four of FK506, as well as seven hydrophobic interactions vs. six of FK506 within the active site residues. These functional residues are highly repetitive and consistent with previously reported active site of model of FK506–FKBP1A complex, and the pharmacophore model was shown feasibly matching with the molecular feature of dolastatin 16.</p>

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