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Connection between antimicrobial venom peptides and bacterial ATP Synthase
Author(s) -
Syed Hiba,
Ahmad Zulfiqar
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.lb104
Subject(s) - atp synthase , antimicrobial , biochemistry , antimicrobial peptides , venom , atpase , escherichia coli , biology , peptide , enzyme , microbiology and biotechnology , chemistry , gene
Background Antibiotic resistance is becoming a huge threat with devastating effects on public health and the global economy. Therefore, finding new alternatives to combat antibiotic resistant microbes is of paramount importance. Selective inhibition of bacterial ATP synthase provides a fascinating opportunity to deal with this ongoing problem. ATP synthase is vital for cellular energy production in almost all organisms from bacteria to man. Inhibition of ATP synthase can deprive cells of ATP resulting in cell death. Many peptides are known to have antimicrobial and antitumor properties. Earlier some peptide were shown to inhibit Escherichia coli ATP synthase establishing that the antimicrobial effects of peptides can be connected to the blocking of ATP generation in bacterial cells. Currently, our lab is exploring the connection between a variety of antimicrobial venom peptides and E. coli ATP synthase. Method The growth properties of wild‐type and mutant E. coli strains along with null strains were verified on fermentable and non‐fermentable carbon sources before harvesting cells in minimal media to isolate ATP synthase. Membrane bound F 1 F o ATP synthase inhibitory studies and E. coli cell growth assays were performed in presence of varied concentrations of natural and modified venom peptides. A null control with deleted ATPase gene was also used in all the studies. Results Our preliminary results show that the natural and modified venom peptides affected degree of inhibition. It seems that inhibitory potency of venom peptides can be enhanced by addition of a c‐terminal NH 2 groups. We also observed that venom peptides follow a differential pattern of inhibition between wild type and mutant ATP synthase. Our initial results also indicate that incremental additions of positive charges can augment the extent of inhibition. Our early results suggest a feasible connection between the antimicrobial properties of venom peptides and bacterial ATP synthase. We are finalizing our preliminary results and we are investigating the synergetic effects of venom peptides on ATP synthase. Conclusions Apparently, antimicrobial venom peptides inhibit E. coli ATP synthase and bind at the βDELSEED‐motif of ATP synthase. Our preliminary data suggests that the inhibitory potency of venom peptides can be augmented through structural modification of venom peptides. Also, selective inhibition of ATP synthase by venom peptides offers a valuable alternative to combat antibiotic resistant bacterial infection. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .