Antimicrobial Microcin C7 Case Study
Abstract- Due to increase in the incidences of drug resistant pathogens, there is a need for the development of alternative drugs against which the microorganisms will not be able to develop resistance. The most promising candidates to be developed as alternative drugs are the antimicrobial peptides. In the present study the antimicrobial peptide Microcin C7 was docked with the catalytic domain of Diphtheria toxin and further the simulational studies were performed to find the stability of the complex. The results were significant and hence it was predicted that further work can be done on antimicrobial peptide to develop it as an altenative drug against Diphtheria toxin.
Keywords-
I. INTRODUCTION
In the last few decades drug resistant bacteria …show more content…
[5-7] Antimicrobial peptides are a part of innate immune system of the organisms. It is found among all the classes of organisms from prokaryotes to eukaryotes in their defence system. [7] Due to several incidences of the conventional antibiotics drug resistant pathogens evolving [4,8,9], the antimicrobial peptides are being developed as an alternative drug against such microorganisms. The microorganisms are less likely to develop resistance against antimicrobial peptides. The antimicrobial peptides act by interacting with the bacterial membranes of the microorganisms. The microorganisms will have to modify a large part of their membranes to become resistant to these antimicrobial peptides which is a very energy consuming process …show more content…
The best docking pose had nine favourable non bond interactions between the toxin and antimicrobial peptide and a global energy -43.23 kcal/mol. The N of Gly22, OG1 of Thr42 and OD1 of Asn69 of Diphtheria toxin form conventional hydrogen bonds with O of Ala6, O of MSE1 and N of MSE1 respectively of Microcin C7. The CE1 of His21 and CA of Ala62 of Diphtheria toxin form carbon hydrogen bond with O of Asn5 and O of Asn7 respectively of Microcin C7. Tyr65 of Diphtheria toxin forms electrostatic non bond with OXT of Asn7 of Microcin C7. The Pi-orbitals of His 21 of Diphtheria toxin form non bond with lone pair of O of Ala6 of Microcin C7. Tyr46 and Tyr65 of Diphtheria toxin form hydrophobic interaction with Arg2 and Ala6 respectively of Microcin
Keywords-
I. INTRODUCTION
In the last few decades drug resistant bacteria …show more content…
[5-7] Antimicrobial peptides are a part of innate immune system of the organisms. It is found among all the classes of organisms from prokaryotes to eukaryotes in their defence system. [7] Due to several incidences of the conventional antibiotics drug resistant pathogens evolving [4,8,9], the antimicrobial peptides are being developed as an alternative drug against such microorganisms. The microorganisms are less likely to develop resistance against antimicrobial peptides. The antimicrobial peptides act by interacting with the bacterial membranes of the microorganisms. The microorganisms will have to modify a large part of their membranes to become resistant to these antimicrobial peptides which is a very energy consuming process …show more content…
The best docking pose had nine favourable non bond interactions between the toxin and antimicrobial peptide and a global energy -43.23 kcal/mol. The N of Gly22, OG1 of Thr42 and OD1 of Asn69 of Diphtheria toxin form conventional hydrogen bonds with O of Ala6, O of MSE1 and N of MSE1 respectively of Microcin C7. The CE1 of His21 and CA of Ala62 of Diphtheria toxin form carbon hydrogen bond with O of Asn5 and O of Asn7 respectively of Microcin C7. Tyr65 of Diphtheria toxin forms electrostatic non bond with OXT of Asn7 of Microcin C7. The Pi-orbitals of His 21 of Diphtheria toxin form non bond with lone pair of O of Ala6 of Microcin C7. Tyr46 and Tyr65 of Diphtheria toxin form hydrophobic interaction with Arg2 and Ala6 respectively of Microcin