Bafilomycin A₁

Bafilomycin A₁ is a bacterial metabolite that has been found in Streptomyces and has diverse biological activities.^1,2,3,4,5 It is an inhibitor of vacuolar H⁺-ATPases (V-ATPases; K_i = 0.5 nM in N. crassa vacuolar membranes) and is greater than 1,000-fold selective for V-ATPases over Na⁺/K⁺-, Ca²⁺-, and H⁺-ATPases.^1,4 Bafilomycin A₁ (100 nM) inhibits autophagosome maturation and protein degradation in H-4-II-E cells.² It inhibits chloroquine-induced apoptosis in primary cerebellar granule neurons (CGNs) but not chloroquine-induced inhibition of macroautophagy.³ Bafilomycin A₁ (100 nM) reduces viral yield in the culture supernatant of Vero E6 and Huh7 cells, as well as HEK293T cells expressing human angiotensin-converting enzyme 2 (ACE2), infected with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).⁵ It also reduces lung RNA copy numbers and viral pneumonia in ACE2 transgenic mice infected with SARS-CoV-2 when administered at a dose of 0.1 mg/kg.

WARNING This product is not for human or veterinary use.

1. Bowman, E.J., Siebers, A., and Altendorf, K. Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA 85(21), 7972-7976 (1988).

2. Yamamoto, A., Tagawa, Y., Yoshimori, T., et al. Bafilomycin A₁ prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct. Funct. 23(1), 33-42 (1998).

3. Shacka, J.J., Klocke, B.J., and Roth, K.A. Autophagy, bafilomycin and cell death: The "A-B-Cs" of plecomacrolide-induced neuroprotection. Autophagy 2(3), 228-230 (2006).

4. Dröse, S., Bindseil, K.U., Bowman, E.J., et al. Inhibitory effect of modified bafilomycins and concanamycins on P- and V-type adenosinetriphosphatases. Biochemistry 32(15), 3902-3906 (1993).

5. Shang, C., Zhuang, X., Zhang, H., et al. Inhibitors of endosomal acidification suppress SARS-CoV-2 replication and relieve viral pneumonia in hACE2 transgenic mice. Virol. J. 18(1), 46 (2021).

Zhang, L.J., Salekeen, R., Soto-Palma, C., et al. Article polyunsaturated lipid senolytics exploit a ferroptotic vulnerability in senescent cells. Cell Press Blue 1(1), 100004 (2026).

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Chen, Y., Lear, T.B., Evankovich, J.W., et al. A high-throughput screen for TMPRSS2 expression identifies FDA-approved compounds that can limit SARS-CoV-2 entry. Nat. Commun. 12(1), 3907 (2021).

Nagakannan, P., Islam, M.I., Conrad, M., et al. Cathepsin B is an excutioner of ferroptosis. Biochim. Biophys. Acta Mol. Cell Res. 1868(3), 118928 (2021).

Soriano-Castell, D., Currais, A., and Maher, P. Defining a pharmacological inhibitor fingerprint for oxytosis/ferroptosis. Free Radic. Biol. Med. S0891-5849(21), (2021).

Kremer, D.M., Nelson, B.S., Lin, L., et al. GOT1 inhibition primes pancreatic cancer for ferroptosis through the autophagic release of labile iron. bioRxiv (2020).