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
Kanokorn Sudto, Patchreenart Saparpakorn, Chompoonuch Tancharoen, Darinee Phromyothin, Supanna Techasakul, Nisachon Khunnawutmanotham, Srunya Vajrodaya, Hui-Ming Ge, Ren Xiang Tan, and Supa Hannongbua** Author for corresponding; e-mail address: fscisph@ku.ac.th
Volume: Vol.46 No.6 (November 2019)
Research Article
DOI:
Received: 23 June 2019, Revised: -, Accepted: 2 August 2019, Published: -
Citation: Sudto K., Saparpakorn P., Tancharoen C., Phromyothin D., Techasakul S., Khunnawutmanotham N., et al., 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, Chiang Mai Journal of Science, 2019; 46(6): 1161-1175.
Abstract
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.