Antibiotics at AG Scientific

DNA Assay

Antibiotics at AG Scientific

A brief introduction to antibiotics

One of our most popular antibiotics anisomycin, is a protein and DNA synthesis inhibitor that specializes in inhibiting the 80S ribosome network (eukaryotes). Anisomycin’s properties of inhibition become activated when concentrations are enough to effect greater than 95% of the 80S ribosome protein synthesis. Additionally, anisomycin works by activating the stress response via the MAP kinase signal transduction pathway.

Anisomycin is most commonly used as an additive to Thayer-Martin agar used for culturing and isolating pathogenic microbial strains including Neisseria gonorrhoeae and Neisseria meningitides. This is because anisomycin will inhibit most other microorganisms, such as C. albicans.

Protein synthesis is a complicated procedure involving many levels and classes of enzymes that align together with many other cytoskeletal structural proteins. Many antibiotics that block microbial protein synthesis interfere either with every 50S subunit of the 70S bacterial ribosome, or the protein production within the 30S subunit. You might think that the aminoacyl-tRNA synthetases, which activate each amino acid necessary for protein synthesis, are the target of these antibiotics, but they are not.

On the other hand, erythromycin inhibits the assembly of 50S subunits and binds to the 23S rRNA part of the 50S ribosome. By obstructing the export tunnel of the 50S polypeptide, the antibiotics clarithromycin, roxithromycin, and ilosone will each stop elongation in the transpeptidation measure of synthesis. Elongation is terminated as soon as peptide formation cannot proceed past the roadblock, which is the macrolide.

Transferase is an integral enzyme associated with translocation, the last part of the elongation cycle. Puromycin will not inhibit the method, but rather competes by performing as an analogue of the 3′-terminal end-of aminoacyl-tRNA, interrupting synthesis and causing premature chain termination.

Among the most frequently employed bactericidal antibiotics are aminoglycosides. This group includes at least eight antibiotics, including streptomycin. The aminoglycosides are known for interfering with the development of the 30S initiation complex. Tetracycline, tobramycin and kanamycin additionally bind to the 30S ribosome and block the synthesis of whichever complex is bigger.

Hygromycin B is an aminoglycoside that specifically binds in an area that has the A, P, and E binding sites of tRNA, to one site inside the 30S subunit. It is theorized that this A site is distorted by this binding and could source as the reason for the potency of hygromycin B to cause misreading of aminoacyl-tRNAs, in addition to avoid the translocation of elongation.

AG Scientific’s Antibiotic Selection Guide

Product # Antibiotic Name Chemical Formula
A-1077 Amphotericin B C47H73NO17
A-1256 17-AAG C31H43N3O8
A-1258 Ascomycin C43H69NO12
A-1414 Ampicillin Sodium Salt C16H18N3O4S•Na
A-1415 Ampicillin Sodium Salt Solution (100 mg/mL) C16H18N3NaO4S
A-2667 Azithromycin C38H72N2O12
A-2757 Ampicillin Trihydrate C16H19N3O4S
A-2651 Avermectin B1A C48H72O14
A-2661 Avermectin B1B C47H70O14
B-1009 Brefeldin A C16H24O4
B-1247 Blasticidin S HCl C17H26N8O5•HCl
B-1247-SOL Blasticidin S HCl Solution C17H26N8O5•HCl
B-2549 Bicyclomycin C12H18N2O7
B-2555 Blasticidin A C58H107NO23
C-1385 Carbenicillin Disodium Salt C17H16N2O6SNa2
C-1386 Carbenicillin Disodium Salt Solution (100 mg/mL) C17H16N2O6SNa2
C-1457 Cefsulodin Sodium Salt C22H19N4NaO8S2•Na
C-1463 Cefotaxime Sodium Salt C16 H16 N5 O7 S2Na
C-2282 Daunorubicin C27H29NO10
C-2603 Candicidin C59H84N2O18
C-2645 Clarithromycin C38H69NO13
D-2525 Dirithromycin C42H78N2O14
D-2539 Doxorubicin hydrochloride C27H30ClNO11
E-2415 Echinocandin B C52H81N7O16
E-2463 Erythromycin A C37H67NO13
F-1030 FK-506 C44H69NO12
F-2425 Fidaxomicin C52H74Cl2O18
F-2427 Filipin C35H58O11
G-1035 G-418 Sulfate, Sterile-Filtered Solution C20H40O10N42H2SO4
G-1047 Geldanamycin C29H40N2O9
G-1067 Gentamycin Sulfate, USP Grade C60H125N15O25S
G-1068-50 Gentamycin Sulfate, 50 mg/mL in DI Water C21H43N5O7•H2SO4
G-1068-10 Gentamycin Sulfate, 10 mg/mL in DI Water C21H43N5O7•H2SO4
H-1012-MU Hygromycin B, Concentrated Solution C20H37N3O13
H-1012-SOLID Hygromycin B Solid C20H37N3O13
H-1012-PBS Hygromycin B, High Purity in PBS Buffer C20H37N3O13
H-1012-DI Hygromycin B in DI Water C20H37N3O13
I-1015 Ionomycin, Calcium Salt C41H72O9•Ca
K-1022 Kanamycin Sulfate C18H36N4O11•H2O4S
K-1023 Kanamycin Sulfate Solution (50 mg/mL) C18H36N4O11•H2O4S
K-1066 Kasugamycin HCl C14H25N3O9•HCl
L-1043 Lovastatin C24H36O5
M-1130 Mitomycin C, in NaCl C15H18N4O5•NaCl
N-2408 Naphthomycin B C39H44ClNO9
N-2409 Nargenicin A1 C28H37NO8
N-2593 Nargenicin B1 C29H39NO10
N-2607 Nogalamycin C39H49NO16
N-2653 Nalidixic Acid Sodium Salt C12H11N2NaO3
O-1060 Oligomycin C45H74O11
O-1063 Oligomycin A C45H74O11
O-1064 Oligomycin B C45H72O12
O-1066 Oligomycin C C45H74O10
O-2545 Oleandomycin C35H61NO12
O-2547 Oligomycin D C44H72O11
O-2549 Oligomycin E C45H72O13
P-1683 Penicillin Steptomycin Solution N/A
R-1014 Resveratrol C14H12O3
R-1018 Rapamycin C51H79NO13
R-2611 Roxithromycin C41H76N2O15
S-2793 Spiramycin C43H74N2O14
T-1016 Tunicamycin C39H64N4O16
T-1206 Tobramycin Sulfate Salt C18H37N5O9•5H2SO4
T-2567 Troleandomycin C41H67NO15
T-2641 Tilmicosin C46H80N2O13
T-2665 Tulathromycin C41H79N3O12
T-2667 Tylosin C46H77NO17
V-1013 Valinomycin  C54H90N6O18
V-2501 Virginiamycin C28H35N3O7 (for M1), C43H49N7O10 (for S1)

Further Reading

1. Sobin, B. A. et al. (1954) J. Am. Chem. Soc. 76, 4053.

2. Jimenez, A. et al. (1979) p. 1-19. In F. E. Hahn (ed.), Antibiotics, vol. 5 part 2. Springer-Verlag, New York, N.Y.

3. Barbacid, M. et al. (1975) J. Mol. Biol93, 449.

4. Kochi, S.K. et al. (1993) Exp. Cell. Res208, 296.

5. Condorelli, G. et al. (2002) J. Biol. Chem. 277, 11013.

6. Cano, E. et al. (1994) Mol. Cell. Biol14, 7352.

7. Cano, E. et al. (1995) J. Cell Sci108, 3599.

8. Chen, D.Âet al. (1996) J. Biol. Chem271, 6328.

9. Ishikawa, Y. and Kitmura, M. (1999) Biochem. Biophys. Res. Commun. 264, 696.

10. Bogoyevitch, M.A. et al. (1995) J. Biol. Chem270, 29710.

11. Sanchez, et al. (1994) Nature 372, 794.

12. Drijard, B. et al. (1994) Cell 76, 1025.

Leave a Reply

Your email address will not be published. Required fields are marked *


*