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A Benzimidazole Carboxamide Derivative, DDB‐506 Inhibits Bacterial Proliferation by Targeting FtsZ
Author(s) -
TIWARI RISHU,
DHAMELIYA TEJAS M.,
CHAKRABORTY ASIT K.,
PANDA DULAL
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.810.10
Subject(s) - ftsz , bacillus subtilis , gtp' , gtpase , cell division , tubulin , biology , microbiology and biotechnology , bacterial cell structure , biochemistry , chemistry , cell , microtubule , bacteria , genetics , enzyme
FtsZ, a conserved cell division protein in prokaryotes has emerged as an attractive target for antibacterial drugs. FtsZ plays a key role in bacterial cell division; therefore targeting FtsZ assembly may be an efficient approach to inhibit bacterial cell division. In this work, we have checked the effect of several benzimidazole carboxamide derivatives on the bacterial cell proliferation. A benzimidazole carboxamide derivative, DDB‐506 was found to inhibit the proliferation of Bacillus subtilis ( B. subtilis ) with an MIC of 6 μM. DDB‐506 increased the length of B. subtilis cells by six times indicating that it inhibits bacterial cytokinesis. Light scattering, sedimentation and electron microscopic analysis of the effects of DDB‐506 on the assembly of Bacillus subtilis FtsZ ( Bs FtsZ) indicated that DDB‐506 inhibits the polymerization of Bs FtsZ in vitro . DDB‐506 also inhibited the GTPase activity of Bs FtsZ. Molecular docking analysis showed that DDB‐506 possibly binds to the nucleotide binding site of Bs FtsZ. DDB‐506 also inhibited the binding of MANT‐GTP, a fluorescent analogue of GTP to FtsZ suggesting that the compound may bind to the GTP binding site of FtsZ. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .