24125-28-8

Basic information

• Product Name: leupeptin acid
• Synonyms: leupeptin acid;Leupeptin【Sigma】;Loupeptin acid;N-Acetyl-Leu-Leu-Arg-OH;N-Acetyl-L-Leu-L-Leu-L-Arg-OH;N-Ac-L-Leu-L-Leu-L-Arg-OH;Nα-[N-(N-Acetyl-L-Leu-)-L-Leu-]-L-Arg-OH
• CAS NO: 24125-28-8
• Molecular Formula: C20H38N6O5
• Molecular Weight: 442.55292
• Mol File: 24125-28-8.mol
• Article Data: 3

Chemical Properties

• Boiling Point: °Cat760mmHg
• Flash Point: °C
• Appearance: /
• Density: 1.26g/cm³
• CAS DataBase Reference: leupeptin acid(CAS DataBase Reference)
• NIST Chemistry Reference: leupeptin acid(24125-28-8)
• EPA Substance Registry System: leupeptin acid(24125-28-8)

Safety Data

• Hazardous Substances Data: 24125-28-8(Hazardous Substances Data)

Upstream product

• 24365-47-7 leupeptin 

Relevant articles and documents

Inhibition properties of free and conjugated leupeptin analogues

Leupeptin is a naturally occurring inhibitor of various proteases, in particular serine proteases. Following its discovery, the inhibitory properties of several other peptidyl argininals have been studied. The specificity of leupeptin is most likely due to the Leu–Leu–Argininal sequence, and its C-terminal aldehyde group has been suggested to enhance the binding efficiency and to be essential for function. The terminal aldehyde group makes the structure less vulnerable to carboxypeptidases. Here, we investigated whether the inhibitory function of leupeptin toward serine proteases is retained after oxidation or reduction of the aldehyde group. The oxidized form, which corresponds to the natural precursor, was shown to be superior to the reduced form in terms of inhibitory properties. However, the original leupeptin possessed enhanced inhibitory properties as compared with the oxidized form. Based on these results, new synthetic leupeptin analogues, 6-aminohexanoic acid (Ahx)–Phe–Leu–Arg–COOH and Ahx–Leu–Leu–Arg–COOH, were prepared by solid-phase peptide synthesis using the Fmoc strategy. In these analogues, the N-terminal capping acetyl group was replaced with a 6-aminohexanoyl group to allow conjugation. The structures of the modified leupeptin and the synthetic peptides were confirmed by mass spectrometry. Determination of the inhibitory properties against trypsin (IEC 3.4.21.4, Chymotrypsin IEC 3.4.21.1) revealed that these further modified tripeptides were tight binding inhibitors to their target enzyme, similar to the naturally occurring leupeptin, with Ki values generally in the micromolar range. The Ahx–Phe–Leu–Arg–COOH analogue was selected for conjugation to inorganic oxide nanoparticles and agarose gel beads. All conjugates exhibited inhibitory activity in the same range as for the free peptides.

Isolation and characterization of leupeptins produced by Actinomycetes.

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