Leupeptin is a natural protease inhibitor with low toxicity to humans. It protects hair cells in the ear from being killed by loud noises and some antibiotics, preventing hearing loss. Leupeptin is used in protein purifications to prevent proteases from degrading the protein of interest. It inhibits endopeptidases and is effective against a broad range of proteases. Leupeptin shows promise in protecting hair cells and preventing severe hearing loss caused by loud noise or certain antibiotics.
Leupeptin is a protease inhibitor naturally produced by some species of Streptomyces soil bacteria and thus inhibits protein degradation. Unlike many synthetic protease inhibitors, it has very low toxicity to humans. This compound has been shown in animal model research to protect the hair cells in the ear from being killed by loud noises and some antibiotics and, in turn, prevents hearing loss. Leupeptin is used extensively during the first part of protein purifications to prevent proteases in the tissue from degrading the protein of interest.
This natural product is a small peptide, a molecule made up of three linked amino acids that has some unusual attributes. The amino group of the compound has an acetyl group – CH3CH2 – on it. Also, the carboxyl group is chemically different from most peptides and proteins, because it has an aldehyde group instead of a carbonyl moiety.
Proteases fall into a number of classes. The first important distinction is whether they cleave at the center of the molecule, like endopeptidases, or they nibble at the ends of molecules, like exopeptidases. Leupeptin inhibits proteases with endopeptidase activity. There are also further classifications based on the structure of the active site, such as cysteine and serine proteases. This protease inhibitor prevents the activity of some of these types of enzymes, such as trypsin and proteinase K, while it is also ineffective with others such as chymotrypsins.
The extent of protease inhibition by leupeptin makes it a very useful compound in biochemical research and large-scale protein production. Generally, when starting to isolate a protein from a biological source, destruction of the tissue releases large numbers of proteases which can begin to degrade the protein of interest. Biochemists usually include a cocktail of protease inhibitors to prevent the protein from being destroyed. Because of its potency, activity on a broad range of proteases, and low toxicity, leupeptin is often a component of such blends.
Ear hair can be destroyed by prolonged exposure to noise above 80 decibels, meningitis, ear infections, some antibiotics and anticancer drugs, aging, and heredity. Studies with animal models have shown that leupeptin shows promise in protecting hair cells and preventing severe hearing loss after subjecting mammals to loud noise or certain antibiotics. Aminoglycoside antibiotics tend to be the type that can cause hearing loss, including drugs like gentamicin and neomycin.
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