(1) Aoyagi, T. et al. (1971) J. Antibiotics 24, 687-694
Effect of Pepstatin on acid proteases.
(2) Umezawa, H. (1976) Methods Enzymol. 45, 678-695
Structures and activities of protease inhibitors of microbial origin.
(3) Katoh, I. et al. (1987) Nature 329, 654-656
Inhibition of retroviral protease activity by an aspartyl proteinase inhibitor.
(4) Von der Helm, K. et al. (1989) FEBS Lett. 247, 349-352
Inhibition of HIV replication in cell culture by the specific aspartic protease inhibitor Pepstatin A.
(5) Menéndez-Arias, L. et al. (1992) J. Biol. Chem. 267, 24134-24139
Purification and characterization of the MMTV protease expressed in Escherichia coli.
(6) Saiga, A. et al. (1993) Arch. Virol. 128, 195-210
The HTLV-1 protease expressed in Escherichia coli possesses aspartic proteinase activity.
Pepstatin was isolated from Streptomyces testaceus and different actinomycetes. It is a strong inhibitor of acidic proteases (''Aspartic Proteases''): Pepsin, HIV and MMTV protease, cathepsin D and renin (1-6). Pepstatin is not a strong toxin (1, 2). The working concentration ranges from 1 μM (0.7 μg/ml) to 5 μM, whereas the MMTV protease requires a higher dose (IC50 = 90 μM, ref. 5). Solutions are stable for approx. 1 week at +4°C or 1 month at -20°C.
Pepstatin may be dissolved in methanol or ethanol at a concentration of 1 mg/ml.. It is of low solubility in ethyl acetate, ether, benzene, chloroform, acetic acid, DMSO, pyridine and water (2). Under the assay conditions described in reference 3 (concentration 1 μM - 1 mM in DMSO), a precipitate of pepstatin A was observed.