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Author: search.filters.author.Saparpakorn, PatchreenartSubject: search.filters.subject.Antimicrobial resistance

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    Item type:Publication,
    Diptoindonesin D, a potent antibacterial activity against gram-positive bacteria, an inhibitor of penicillin-binding protein 2a from the stem bark of Shorea roxburghii G.Don
    (2019-11-01)
    Sudto, Kanokorn
    ;
    Saparpakorn, Patchreenart
    ;
    Tancharoen, Chompoonuch
    ;
    Phromyothin, Darinee
    ;
    Techasakul, Supanna
    The emergence and spread of antimicrobial resistance (AMR) is a serious threat to public human health. The challenge now is an urgent need to new potent antibiotics combating AMR which can be an effective way to solve the crisis. A new potent antibacterial activity of diptoindonesin D, together with four known compounds as hopeafuran, α-viniferan, hopeahainol A and hopeahainol C were isolated from the stem bark of Shorea roxburghii G. Don in Khon Kaen province, Thailand. Diptoindonesin D were screened for antimicrobial activity and possesses significant activity minimum inhibitory concentrations (MIC) values of 4.68 and 9.37 μg/mL against Staphylococcus epidermidis and Staphylococcus aureus, respectively. The absolute configuration of diptoindonesin D were evaluated by circular dichroism (ECD) calculations. The ECD results indicated that the possible configuration of diptoindonesin D should be R-configuration. Furthermore, reverse docking was performed to identify the protein target of diptoindonesin D based on four scoring functions using GOLD program. This investigation is the first time that reveals interaction between diptoindonesin D and its binding with cell wall synthesis protein targets. The results highlighted that, penicillin-binding protein 2a (PBP2a), an antibacterial cell wall, might be the potential target for the binding of diptoindonesin D. The obtained results can be useful as a guideline for the development of effective diptoindonesin D as a PBP2a inhibitor.