H-Asp(AMC)-OH

H-Asp(AMC)-OH is an L-aspartic acid derivative bearing an amide-linked 7-amino-4-methylcoumarin (AMC) reporter at the side chain, retaining the native α-amino and α-carboxyl functionality in a free amino acid form. The molecule contains a stereogenic α-carbon consistent with L-configuration, a side-chain carboxamide that is conjugated to the coumarin fluorophore, and a coumarin aromatic system capable of strong fluorescence upon appropriate excitation. The presence of both an α-carboxylic acid and an α-amino group makes it compatible with amino acid coupling chemistry, while the AMC moiety introduces a stable, conjugation-ready chromophore that can participate in analytical and biochemical readouts. The side-chain functionalization changes the reactivity profile relative to unmodified aspartate by converting the side-chain carboxylic acid into a reporter amide, enabling controlled peptide incorporation and downstream enzymatic or chemical monitoring.

1. Peptide Synthesis

H-Asp(AMC)-OH is suitable for peptide building block preparation where an aspartate residue bearing a coumarin reporter is required at a defined position. The protected amino acid derivative format is not used here because the compound presents free α-amino and α-carboxyl groups, so peptide coupling strategies typically rely on temporary protection of the α-amino group and activation of the α-carboxyl to form amide bonds. The side-chain AMC amide remains intact under standard peptide coupling conditions, allowing the coumarin label to survive incorporation into peptide chains and to report sequence-dependent processing. Peptides containing H-Asp(AMC)-OH can be used to generate defined substrates for cleavage studies, to build fluorescent peptide standards, and to support structure-activity relationship studies where aspartate positioning and side-chain electronics matter.

2. Chemical Biology Assays

H-Asp(AMC)-OH serves as a fluorescence-enabled amino acid probe for chemical biology workflows that monitor enzymatic activity or binding events through coumarin emission. The AMC reporter is conjugated to the aspartate side chain as an amide, which can be engineered into peptide or linker architectures to translate biochemical recognition into a measurable optical signal. The L-aspartate stereochemistry can be leveraged to maintain stereochemical fidelity in substrate analogs for proteases, amidases, or other enzymes that recognize aspartate-containing motifs. Downstream derivatization can convert the α-functionalities into protected or activated forms for incorporation into assay substrates, enabling quantitative readouts based on coumarin fluorescence changes.

3. Protein Engineering Substrates

H-Asp(AMC)-OH can be applied in protein engineering and enzyme-substrate design where an aspartate-containing recognition element must be traced with a fluorescent tag. The molecule's α-amino acid backbone supports incorporation into peptide segments that mimic native aspartate environments while maintaining the coumarin reporter on the side chain. The AMC amide linkage provides a chemically stable handle for constructing substrate libraries used to probe specificity, cleavage site preferences, or catalytic mechanism hypotheses in a sequence-controlled manner. Fabrication of labeled protein fragments or peptide substrates from H-Asp(AMC)-OH supports downstream analytical characterization and comparative studies of engineered variants.

4. Analytical Fluorescent Standards

H-Asp(AMC)-OH is well aligned with analytical research requiring coumarin-based fluorescence standards and reference materials. The coumarin chromophore provides a strong spectroscopic signature, while the amino acid framework supports conversion into derivatives that match chromatographic behavior of peptide analytes. The presence of both α-carboxylic acid and α-amino functionality enables preparation of calibration compounds, internal standards, or derivatized forms for LC-MS compatible quantitation strategies. Coumarin-labeled aspartate analogs derived from H-Asp(AMC)-OH can also be used to validate assay sensitivity in biochemical workflows that rely on fluorescence readouts.

5. Fine Chemical Synthesis Intermediate

H-Asp(AMC)-OH functions as a chiral amino acid intermediate for the synthesis of coumarin-tagged building blocks and labeled reagents in fine chemical production. The L-aspartate stereocenter and the side-chain AMC amide define a fixed stereochemical and functional motif that can be carried through protection, activation, and coupling sequences to generate peptide coupling partners or specialized labeled fragments. The α-carboxylic acid can be transformed into activated esters or activated acids, while the α-amino group can be temporarily protected to control chemoselectivity during downstream assembly. The resulting labeled intermediates can feed into specialty chemical production routes for fluorescent probes, peptide standards, and research-grade substrates used across amino acid chemistry and applied biochemical instrumentation.

1. Extended exenatide administration enhances lipid metabolism and exacerbates pancreatic injury in mice on a high fat, high carbohydrate diet

2. Quantitative Analysis of Ligands Effects on Bioefficacy of Nanoemulsion encapsulating Depigmenting Active

3. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry

4. GLP-1, exendin-4 and C-peptide regulate pancreatic islet microcirculation, insulin secretion and glucose tolerance in rats

5. Myotropic activity of allatostatins in tenebrionid beetles