Investigation of β-lactam antibacterial drugs, β-lactamases, and penicillin-binding proteins with fluorescence polarization and anisotropy: a review.
نویسنده
چکیده
This review covers the uses of fluorescence polarization and anisotropy for the investigation of bacterial penicillin binding proteins (PBPs), which are the targets of β-lactam antibacterial drugs (penicillins, cephalosporins, carbapenems, and monobactams), and of the β-lactamase enzymes that destroy these drugs and help to render bacterial pathogens resistant to them. Fluorescence polarization and anisotropy-based methods for quantitation of β-lactam drugs are also reviewed. A particular emphasis is on methods for quantitative measurement of the interactions of β-lactams and other inhibitors with PBPs and β-lactamases.
منابع مشابه
Investigation of β-lactam antibacterial drugs, β- lactamases, and penicillin-binding proteins with fluorescence polarization and anisotropy: a review
This review covers the uses of fluorescence polarization and anisotropy for the investigation of bacterial penicillin binding proteins (PBPs), which are the targets of β-lactam antibacterial drugs (penicillins, cephalosporins, carbapenems, and monobactams), and of the β-lactamase enzymes that destroy these drugs and help to render bacterial pathogens resistant to them. Fluorescence polarization...
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II. The occurrence of modified penicillin-binding sites Modified PBPs have a lower affinity for β-lactam antibiotics, requiring clinically unattainable concentrations of the drug to effect its bactericidal activity Example: penicillin resistance in Streptococcus pneumoniae (pneumococcus) is caused by altered PBPs I. Production of β-lactamases This family of enzymes can inactivate penicillins by...
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ورودعنوان ژورنال:
- Methods and applications in fluorescence
دوره 4 2 شماره
صفحات -
تاریخ انتشار 2016