BAFILOMYCIN A1 ??

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Bafilomycin A₁ is a fungal metabolite that has been found in Streptomyces and has diverse biological activities. 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. Bafilomycin A₁ (100 nM) inhibits autophagosome maturation and protein degradation in H-4-II-E cells. It inhibits chloroquine-induced apoptosis in primary cerebellar granule neurons (CGNs) but not chloroquine-induced inhibition of macroautophagy. 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). 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.

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white to off-white powder

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Bafilomycin A1 is a member of a potent family of macrocyclic lactones with broad spectrum biological activity, including activity against bacteria, yeast, fungi, nematodes, insects and tumour cell lines. Bafilomycin A1 is an inhibitor of vacuolar-type ATPase.

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ChEBI: The most used of the bafilomycins, a family of toxic macrolide antibiotics derived from Streptomyces griseus.

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A macrolide antibiotic that acts as a specific inhibitor of vacuolar-type H⁺-ATPase (V-type; K_i = 500 pM). A valuable tool for distinguishing among different types of ATPases. Blocks lysosomal cholesterol trafficking in macrophages and is known to interfere with pH regulation in brain cells. Exhibits cytotoxic effects on a number of cell lines in a cell viability assay. Reported to selectively inhibit β-secretase, an enzyme involved in the processing of amyloid precursor protein (APP). The InSolution format with a purity of ≥97% by HPLC in 90% DMSO is also available (Cat. No. 508409).

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Highly potent, selective inhibitor of vacuolar H + -ATPases (IC 50 = 500 pM as measured in chromaffin granule membranes). Selective over other ATP hydrolyzing enzymes such as F-ATPases, Ca 2+ -ATPases, Na + /K + -ATPases and plasma membrane H + -ATPases.

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