Antibiotic drug resistance is a serious issue for the treatment of bacterial infection. Understanding the resistance to antibiotics is a key issue for developing new drugs. We used penicillin and sulbactam as model antibiotics to study their interaction with model membranes. Cholesterol was used to target the membrane for comparison with the well-known insertion model. Lamellar X-ray diffraction (LXD) was used to determine membrane thickness using successive drug-to-lipid molar ratios. The aspiration method for a single giant unilamellar vesicle (GUV) was used to monitor the kinetic binding process of antibiotic-membrane interactions in an aqueous solution. Both penicillin and sulbactam are found positioned outside the model membrane, while cholesterol inserts perpendicularly into the hydrophobic region of the membrane in aqueous solution. This result provides structural insights for understanding the antibiotic-membrane interaction and the mechanism of antibiotics.
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http://dx.doi.org/10.1016/j.fob.2015.06.006 | DOI Listing |
Biosens Bioelectron
May 2022
Robert F. Smith School of Chemical and Biomolecular Engineering, Cornell University, Ithaca, NY, USA; Meinig School of Biomedical Engineering, Cornell University, Ithaca, NY, USA. Electronic address:
Antibiotic resistance is a growing global health concern due to the decreasing number of antibiotics available for therapeutic use as more drug-resistant bacteria develop. Changes in the membrane properties of Gram-negative bacteria can influence their response to antibiotics and give rise to resistance. Thus, understanding the interactions between the bacterial membrane and antibiotics is important for elucidating microbial membrane properties to use for designing novel antimicrobial drugs.
View Article and Find Full Text PDFFEBS Open Bio
July 2015
National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan ; Department of Physics, National Central University, Jhongli 32001, Taiwan.
Antibiotic drug resistance is a serious issue for the treatment of bacterial infection. Understanding the resistance to antibiotics is a key issue for developing new drugs. We used penicillin and sulbactam as model antibiotics to study their interaction with model membranes.
View Article and Find Full Text PDFEur Biophys J
August 2012
Department of Biophysics, University of Life Sciences in Lublin, Akademicka 13, 20-950 Lublin, Poland.
Langmuir monolayers of amphotericin B (AmB) were investigated by recording π-A isotherms under different pH conditions. To gain a better insight into antibiotic-membrane interactions they were monitored by use of the ATR-FTIR spectroscopy. It was observed for AmB monolayers that the limiting molecular area was larger at high than at neutral pH.
View Article and Find Full Text PDFJ Phys Chem B
December 2010
Department of Chemistry, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Interactions between membranes and amyloid proteins are believed to be a major factor contributing to pathogenesis in amyloid diseases. Furthermore, membranes have been shown to closely affect fibrillation processes of varied amyloidogenic peptides. Here we describe an intriguing phenomenon in which bilayer-induced fibrillation of human calcitonin (hCT) gave rise to significant inhibition of membrane interactions of alamethicin, an antibiotic, membrane-permeating peptide.
View Article and Find Full Text PDFLangmuir
October 2008
Department of Physics, Indian Institute of Science, Bangalore 560012, India.
The aggregation properties of an antibiotic membrane-active peptide alamethicin at the air-water interface have been studied using interfacial rheology and fluorescence microscopy techniques. Fluorescence microscopy of alamethicin monolayers revealed a coexistence of liquid expanded (LE) and solid phases at the surface concentrations studied. Interfacial oscillatory shear measurements on alamethicin monolayers indicate that its viscoelastic properties are determined by the area fraction of the solid domains.
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