Free energy decomposition of caro outer membrane protein of acinetobacter baumannii
Citation
Sarıyer, E. (2022). Free Energy Decomposition of CarO Outer Membrane Protein of Acinetobacter baumannii. Cumhuriyet Science Journal, 43(1), 20–26. Abstract
The increase in the number of antibiotic-resistant microorganisms reported today has made this issue one of
the main topics of all institutes. Acineteobacter baumanni is a species that is on the list of the WHO and plays
an important role, especially in hospital-acquired infections. CarO outer membrane protein, which regulates the
passage of small molecules and some antibiotics into the periplasmic space and is associated with carbapenem
resistance, has been identified in A. baumannii. In this study, residues that contribute to the binding energy of
imipenem to different types of CarO proteins were identified. In addition, energy decomposition was compared
when Biapenem, Ertapenem, Imipenem, Faropenem, and Meropenem were docked to ATCC-17978 CarO
protein separately. As a result of this study, it was determined that generally charged residues had a negative
effect on binding affinity, but hydrophobic and uncharged residues had a positive effect. In addition, in
ertapenem, faropenem, and meropenem-bound complexes, charged residues increased the affinity and caused
the interaction between carbapenems and CarO to be continuous and tight. It was predicted that the residues
determined in this study would be precursors to mutagenesis studies and could also be an example for similar
studies.