H-L-Asp(Bzl)-AMC*HCl

H-L-Asp(Bzl)-AMC*HCl is an L-aspartic acid derivative bearing a benzyl-protected side-chain carboxyl group (Asp(Bzl)) and an amide-linked 7-amino-4-methylcoumarin (AMC) reporter, supplied as the hydrochloride salt. The molecule contains a stereodefined α-amino acid core with a chiral center, a benzyl ester that can be removed under hydrogenolysis-compatible conditions, and a coumarin fluorophore that enables sensitive signal generation upon enzymatic or chemical cleavage. The AMC amide linkage introduces a stable reporter handle for assay readouts and analytical quantification, while the hydrochloride form improves handling of the basic coumarin amine motif. The combination of a protected side-chain and an AMC leaving-group surrogate makes this compound a practical biochemical research intermediate and a substrate-format building block for peptide and amino acid chemistry workflows.

1. Fluorogenic Enzyme Assays

H-L-Asp(Bzl)-AMC*HCl is applied in enzymology and chemical biology as a fluorogenic substrate format for protease- or peptidase-like activities that recognize Asp-containing motifs. The Asp(Bzl) side-chain carboxyl protection and the AMC amide reporter together create a cleavage-dependent fluorescence signal pathway, where side-chain deprotection is not required for assay readout but can be leveraged for downstream derivatization. The defined L-configuration at the α-carbon supports stereochemical recognition by enzyme active sites, enabling structure-function studies on substrate preferences. The coumarin reporter supports high-sensitivity monitoring compatible with plate-based formats, and the HCl salt form helps maintain reproducible solubility for routine screening and method development.

2. Protected Amino Acid Chemistry

H-L-Asp(Bzl)-AMC*HCl is utilized in protected amino acid synthesis planning because the benzyl-protected aspartate side chain provides a clear orthogonal handle for selective deprotection strategies. The molecule's Asp(Bzl) functionality models the protection logic used in peptide coupling chemistry, where side-chain carboxyl protection can be maintained during N-terminal activation and then removed to expose a free acidic group for subsequent steps. The AMC-linked amide can be retained during protection/deprotection sequences when the reporter is needed as a downstream analytical tag, or transformed when converting the compound into other aspartate derivatives. The chiral amino acid backbone and protected carboxyl group pattern make it suitable as an intermediate reference material for building protected Asp-containing scaffolds and for validating protecting-group compatibility in synthetic routes.

3. Peptide Coupling Substrate Design

H-L-Asp(Bzl)-AMC*HCl is relevant to peptide science and substrate engineering for constructing Asp-centered peptide analogs used in mechanistic studies. The amino acid architecture provides a stereodefined Asp residue equivalent, while the benzyl ester protects the side-chain carboxyl to control chemoselectivity during coupling or further functionalization. The AMC reporter acts as a measurable tag that can be incorporated into peptide-like constructs to monitor cleavage at specific bonds or to compare sequence-dependent processing by enzymes. The hydrochloride salt form supports handling in aqueous assay-adjacent conditions, and the protected side-chain pattern can guide how Asp-containing residues are protected in multi-step peptide building-block preparations.

4. Analytical Research Standards

H-L-Asp(Bzl)-AMC*HCl is employed in analytical chemistry and biochemical method development as a defined fluorescent reference material for quantifying reporter release and calibrating assay response. The coumarin fluorophore embedded in the AMC amide provides a stable spectroscopic readout, while the Asp(Bzl) protected side chain and L-stereochemistry help maintain consistent chemical identity across experiments. The HCl salt form improves reproducibility in sample preparation, which is important for comparing reaction progress across runs and for validating analytical workflows. Downstream derivatization of the benzyl-protected carboxyl group can enable preparation of structurally related standards, supporting method transfer and specificity testing in amino acid and peptide analytical studies.

5. Fine Chemical Synthesis Intermediate

H-L-Asp(Bzl)-AMC*HCl serves as a synthetic intermediate in fine chemical production where an aspartate-derived, reporter-tagged scaffold is required for downstream molecule generation. The benzyl-protected side-chain carboxyl group provides a controllable functional-group stage for conversion into other Asp derivatives, including carboxylate-exposed forms after deprotection, while the AMC amide maintains a robust reporter functionality for tracking transformations. The chiral amino acid backbone supports stereochemically defined intermediate manufacture, which can be important for producing consistent peptide building blocks and amino acid analogs at scale. The compound's structural features align with industrially relevant protecting-group strategies and can be integrated into process chemistry routes for preparing fluorescent substrates, tagged intermediates, and related aspartate-based reagents.

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