4.7 Article

Exploring the quorum sensing inhibition of isolated chrysin from Penicillium chrysogenum DXY-1

期刊

BIOORGANIC CHEMISTRY
卷 111, 期 -, 页码 -

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2021.104894

关键词

Chrysin; Quorum sensing; Inhibitor; CviR; Penicillium chrysogenum DXY-1

资金

  1. Natural Science Foundation of China [U1805234, 22007013]
  2. Natural Science Foundation of Fujian Province of China [2019J01264, 2020J05033]
  3. Program for Innovative Research Team in Science and Technology in Fujian Province University
  4. Special Funds of the Central Government Guiding Local Science and Technology Development [2020L3008]
  5. Science and Technology Program under Fujian Provincial Department of Education [JAT190078]
  6. Scientific Research Startup Fund for HighLevel Talents in Fujian Normal University [004828]
  7. 100 Talents Program of Fujian Province

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The study demonstrated that chrysin isolated from Penicillium chrysogenum DXY-1 exhibited anti-quorum sensing activity, inhibiting bacterial quorum sensing system by competing with natural signal molecules for binding to the receptor. This interference prevented the binding of signal molecules to the receptor, ultimately inhibiting bacterial growth and biofilm formation.
We recently and for the first time reported that ethyl acetate extracts isolated from Penicillium chrysogenum DXY-1 exhibited anti-quorum sensing (anti-QS) activity. Herein, another active molecule in the extracts was identified as chrysin by NMR and MS. A 20 mu g/mL dose of chrysin inhibited violacein production regulated by QS in C. violaceum CV026 by 31.6%. A 40 mu g/mL dose of chrysin suppressed pyocyanin production, elastase activity, proteolytic activity, and biofilm formation regulated by QS in P. aeruginosa PA01 by 41.4%, 13.8%, 8.3%, and 42.4%, respectively. And chrysin could inhibit the swarming activity of P. aeruginosa PA01. Further, molecular docking and CD analysis were used to address the mechanism of chrysin's activity in C. violaceum. Molecular docking results revealed that chrysin suppresses QS system by competing with the natural signal molecule C6HSL for binding to the same pocket of CviR receptor. At the same time, CD results also showed that chrysin could change the secondary structure composition of CviR, which greatly prevented the binding of C6HSL/CviR, and further playing its role on inhibiting bacterial QS system. All these data demonstate that chrysin may be used as a potential QS inhibitor to tackle increasing drug resistance.

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