Cellular FLICE (FADD-like IL-1beta-converting enzyme)-inhibitory protein (c-FLIP) is major resistant and inhibitor factor of TRAIL mediated apoptosis in cancer cells. Generally cFLIP is over expressed in all cancer cells and act as anti apoptotic agent, hence it became one of the important targets for cancer therapy. Fungal peptides are having very good pharmaceutical value and reported for various treatment. In present investigation, we described the binding affinity of fungal peptides with cFLIP. Four fungal peptides Pneumocandin B0, Aureobasidin G, WF 11899A, Echinocandin B structures were retrieved pubchem database and cFLIP protein structure was retrieved from Protein Data Bank. Docking studies were carryout by using Hex 8.0.0. Their interactions and binding interface were identified by Ligplot 1.4.5. All four fungal peptides are having binding affinity with cFLIP, among them Pneumocandin B0 showed highest binding energy value of -455.18, having two hydrogen and nine hydrophobic bonds with cFLIP. Whereas, Aureobasidin G exposed energy value of -414.96, Ligpolt analysis showed three hydrogen and seven hydrophobic bonds. WF 11899A binding energy was found to be -377.18, one hydrogen and eight hydrophobic bonds were identified with cFLIP interaction. Echinocandin B was having least binding affinity -342.59 and having only eight hydrophobic bonds. Further in-vitro and in-vivo study is needed to confirm their inhibitor effect on cFLIP.
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