L-Leucine 4-methoxy-β-naphthylamide is a substrate for aminopeptidase M and leucine aminopeptidase.

Aminopeptidases are enzymes catalyzing the cleavage of amino acids from the amino terminus (N-terminus) of proteins or peptides. Aminopeptidases are distributed widely throughout the animal and plant kingdoms and are present in various subcellular organelles, in cytosol, as well as membrane components.

In vitro: L-Leucine 4-methoxy-β-naphthylamide was identified as a cell-permeable substrate for aminopeptidase M and leucine aminopeptidase that was developed for intracellular analysis of protease activities [1]. In a previous method-developing study, peptide derivatives of 4-methoxy-β-naphthylamine including L-leucine 4-methoxy-β-naphthylamide were incubated in microtiter plates together with nitrosalicylaldehyde. Selectivity was achieved by running parallel assays containing inhibitors partially selective for each of peptide derivatives. This method was successfully validated by measurements in cells isolated from cathepsin B-/--, K-/--, and L-/-- mice [2].

In vivo: Up to now, there is no animal in vivo data reported.

Clinical trial: So far, no clinical study has been conducted.

References:

[1] Monis, B. ,Wasserkrug, H. and Seligman, A.M. Comparison of fixatives and substrates for aminopeptidase. Journal of Histochemistry and Cytochemistry 13(6), 503-509 (1965).

[2] Rüttger, A. ,Mollenhauer, J.,Lser, R., et al. Microplate assay for quantitative determination of cathepsin activities in viable cells using derivatives of 4-methoxy-β-naphthylamide. Biotechniques 41(4), 469-473 (2006).

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