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    Ariel Chen
    Two compounds, CB5978818 and CB5225540, were found to inhibit the activity of ricin toxin's RTA protein at concentrations that were not cytotoxic. CB5225540 showed the best inhibition of ricin at 25 uM, reducing its activity by 90%. These compounds could be modified to increase their binding affinity for ricin while decreasing cytotoxicity, and represent novel platforms for developing anti-ricin compounds compared to previous known inhibitors. The virtual screening method used to identify these compounds was deemed successful.

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    Two compounds, CB5978818 and CB5225540, were found to inhibit the activity of ricin toxin's RTA protein at concentrations that were not cytotoxic. CB5225540 showed the best inhibition of ricin at 25 uM, reducing its activity by 90%. These compounds could be modified to increase their binding affinity for ricin while decreasing cytotoxicity, and represent novel platforms for developing anti-ricin compounds compared to previous known inhibitors. The virtual screening method used to identify these compounds was deemed successful.

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    ricin virtual screening

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    Two compounds, CB5978818 and CB5225540, were found to inhibit the activity of ricin toxin's RTA protein at concentrations that were not cytotoxic. CB5225540 showed the best inhibition of ricin at 25 uM, reducing its activity by 90%. These compounds could be modified to increase their binding affinity for ricin while decreasing cytotoxicity, and represent novel platforms for developing anti-ricin compounds compared to previous known inhibitors. The virtual screening method used to identify these compounds was deemed successful.

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    13 views3 pages

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    Ariel Chen
    Two compounds, CB5978818 and CB5225540, were found to inhibit the activity of ricin toxin's RTA protein at concentrations that were not cytotoxic. CB5225540 showed the best inhibition of ricin at 25 uM, reducing its activity by 90%. These compounds could be modified to increase their binding affinity for ricin while decreasing cytotoxicity, and represent novel platforms for developing anti-ricin compounds compared to previous known inhibitors. The virtual screening method used to identify these compounds was deemed successful.

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    Cell-based assay

    Of the six compounds that inhibited RTA activity, two inhibited ricin However both cytotoxic at higher concentrations CB5225540 had best inhibition, ricin 90% inhibited at 25 uM

    CB5978818

    CB5225540

    Cell-based assay
    The other compounds that inhibited RTA activity likely did not inhibit ricin because it was unable to enter cell into cytoplasm

    Conclusion
    The two compounds (CB5978818 and CB5225540) can be further modified to increase binding affinity and decrease cytotoxicity Treated as platforms for developing anti-ricin coumpounds Both are noveldifferent from previous known inhibitors of ricin Success of the virtual screening method

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