Bordetella pertussis Inhibitors
Bordetella pertussis inhibitors serve to obstruct the bacterial growth and virulence by targeting various biochemical and cellular pathways integral to its lifecycle. The primary methods include inhibition of protein synthesis, interference with DNA replication, and disruption of membrane integrity. For example, antibiotics such as Azithromycin and Erythromycin are macrolides that bind to the 50S ribosomal subunit, effectively inhibiting protein translation. This process limits the production of Bordetella pertussis virulence factors and essential proteins. Another class of inhibitors, represented by Auranofin, targets thioredoxin reductase. By impairing bacterial redox homeostasis, this action compromises the functionality of bacterial proteins.
Similarly, agents like Berberine and Triclosan hit other cellular pathways crucial for bacterial growth and survival. Berberine inhibits the FtsZ protein, thus disrupting bacterial cell division and suppressing the bacterium's ability to propagate. Triclosan targets the FabI enzyme, interfering with fatty acid synthesis, an essential component for membrane integrity. Quinolones like Ciprofloxacin inhibit DNA gyrase and topoisomerase IV, enzymes critical for DNA replication and repair. By disrupting these pathways, these inhibitors block the bacterial lifecycle and quell the synthesis of proteins vital for virulence, thereby leading to a significant reduction in Bordetella pertussis activity.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Azithromycin | 83905-01-5 | sc-254949 sc-254949A sc-254949B sc-254949C sc-254949D | 25 mg 50 mg 500 mg 1 g 5 g | $52.00 $103.00 $260.00 $364.00 $728.00 | 17 | |
Macrolide antibiotic that inhibits bacterial protein synthesis by binding to 50S ribosomal subunit, suppressing the expression of virulence factors in Bordetella pertussis. | ||||||
Erythromycin | 114-07-8 | sc-204742 sc-204742A sc-204742B sc-204742C | 5 g 25 g 100 g 1 kg | $57.00 $245.00 $831.00 $1331.00 | 4 | |
Another macrolide that inhibits 50S ribosomal subunit, thereby hindering the translation of essential proteins, including those involved in virulence of Bordetella pertussis. | ||||||
Clarithromycin | 81103-11-9 | sc-205634 sc-205634A | 100 mg 250 mg | $77.00 $122.00 | 1 | |
Inhibits bacterial ribosome 50S subunit, affecting protein synthesis and downregulating the pertussis toxin production. | ||||||
Chloramphenicol | 56-75-7 | sc-3594 | 25 g | $90.00 | 10 | |
Inhibits bacterial ribosome 50S subunit, ceasing protein synthesis and blocking factors necessary for adhesion and invasion. | ||||||
Doxycycline-d6 | 564-25-0 unlabeled | sc-218274 | 1 mg | $16500.00 | ||
Tetracycline antibiotic that interferes with the 30S ribosomal subunit, disrupting bacterial protein synthesis and suppressing virulence traits such as tracheal colonization. | ||||||
Berberine | 2086-83-1 | sc-507337 | 250 mg | $92.00 | 1 | |
Alkaloid that inhibits bacterial FtsZ protein, disrupting cell division and thereby affecting the life cycle of Bordetella pertussis. | ||||||
Auranofin | 34031-32-8 | sc-202476 sc-202476A sc-202476B | 25 mg 100 mg 2 g | $153.00 $214.00 $4000.00 | 39 | |
Thioredoxin reductase inhibitor that impairs bacterial redox homeostasis, compromising the integrity and function of Bordetella pertussis proteins. | ||||||
Triclosan | 3380-34-5 | sc-220326 sc-220326A | 10 g 100 g | $141.00 $408.00 | ||
Inhibits enoyl-acyl carrier protein reductase (FabI), disrupting fatty acid synthesis, essential for membrane integrity and function. | ||||||
Ciprofloxacin | 85721-33-1 | sc-217900 | 1 g | $43.00 | 8 | |
Inhibits bacterial DNA gyrase and topoisomerase IV, which are crucial for DNA replication and repair. This impairs the bacterial lifecycle and the synthesis of proteins important for virulence. | ||||||
Ampicillin | 69-53-4 | sc-210812 sc-210812A sc-210812B sc-210812C sc-210812D | 100 mg 1 g 5 g 25 g 100 g | $31.00 $101.00 $153.00 $115.00 $408.00 | 11 | |
Inhibits bacterial cell wall synthesis by targeting penicillin-binding proteins, disrupting cellular integrity and making the bacterium more susceptible to osmotic lysis. | ||||||