Pub. Date : 2022 Mar 1
PMID : 34896074
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Exploring the permeation of fluoroquinolone metalloantibiotics across outer membrane porins by combining molecular dynamics simulations and a porin-mimetic in vitro model. | Fluoroquinolones | voltage dependent anion channel 1 | Homo sapiens |
| 2 | Porin channels are crucial for the permeation of fluoroquinolones across the outer membrane of Gram-negative bacteria and modifications in porin expression are an important mechanism of bacterial resistance. | Fluoroquinolones | voltage dependent anion channel 1 | Homo sapiens |
| 3 | Porin channels are crucial for the permeation of fluoroquinolones across the outer membrane of Gram-negative bacteria and modifications in porin expression are an important mechanism of bacterial resistance. | Fluoroquinolones | voltage dependent anion channel 1 | Homo sapiens |
| 4 | Molecular dynamics simulations showed that the translocation of the metalloantibiotic through this porin is less favorable than that of free fluoroquinolone, as it presented a much larger free energy barrier to cross the narrow constriction region of the pore. | Fluoroquinolones | voltage dependent anion channel 1 | Homo sapiens |
| 5 | Lastly, permeability studies of different fluoroquinolones and their respective copper complexes using a porin-mimetic in vitro model corroborated the lower rate of permeation for the metalloantibiotics relative to the free antibiotics. | Fluoroquinolones | voltage dependent anion channel 1 | Homo sapiens |