Abz-Gly-OH · HCl contains an aminobenzoic acid (Abz) aromatic moiety linked to glycine, forming a free amino acid derivative present as a hydrochloride salt; the molecule bears both an amino group and a carboxylic acid functionality, with the Abz group providing a conjugatable aromatic handle for spectroscopic or labeling contexts. The HCl counterion associates with the basic amino functionality, and the Abz-glycine connectivity defines a non-proteinogenic, peptide-relevant building block that can be used without introducing additional side-chain reactivity beyond glycine's hydrogen substituent. Abz-Gly-OH · HCl is employed in peptide and amide synthesis as a substrate or precursor for constructing Abz-containing peptides and for analytical method development where an aromatic reporter group is used to monitor chemical transformations or peptide-related structures.
CAT No: CP26897
CAS No:256657-23-5
Synonyms/Alias:256657-23-5;Abz-Gly-OHHCl;ABZ-GLY-OHHCL;C9H10N2O3.HCl;2-Amino-hippuricacid.HCl;6070AH
Abz-Gly-OH · HCl is an amino acid derivative combining glycine with the Abz (anthraniloyl/aminobenzoyl) aromatic fluorophore, supplied as the hydrochloride salt to support handling and salt-form solubility. This structure is widely used in peptide and protease assay workflows where the Abz group provides a convenient spectroscopic handle for monitoring cleavage, release, or labeling outcomes. The free carboxylic acid and amino functionality make it a practical building block for assembling Abz-containing peptide substrates and standards.
1. Fluorogenic Protease Substrates
Abz-Gly-OH · HCl is frequently used by enzymology and chemical biology groups to prepare fluorogenic peptide substrates that report proteolytic cleavage through fluorescence changes associated with the Abz chromophore. Researchers incorporate the Abz-Gly motif into short peptides used to screen or characterize protease activity in vitro, enabling kinetic readouts that are compatible with plate-based fluorescence measurements. The hydrochloride salt form helps maintain consistent reagent performance during peptide substrate preparation and downstream assay setup, particularly when working with small, highly functionalized peptide fragments.
2. Peptide Library Building Block
Abz-Gly-OH · HCl serves as a convenient Abz-bearing glycine building block for constructing peptide libraries and positional variants used in structure-activity and substrate specificity studies. Peptide chemists and medicinal chemistry teams use Abz-containing intermediates to generate defined N-terminus or internal labeling patterns that can be tracked by fluorescence once integrated into longer sequences. The presence of the glycine backbone supports straightforward incorporation into peptide constructs, while the Abz group provides a built-in spectroscopic tag for verifying assembly, monitoring fragment behavior, or comparing relative cleavage/processing across analogs.
3. Analytical Standards And Controls
Abz-Gly-OH · HCl is commonly used to prepare analytical standards and assay controls for fluorescence-based peptide workflows, including calibration materials for Abz-containing fragments and reference compounds for method validation. Analytical chemists use the Abz-Gly motif to confirm identity and performance of Abz-labeled peptide substrates, cleavage products, or derivatized intermediates during LC-fluorescence or fluorescence-only readouts. Supplying the compound as a defined hydrochloride salt supports reproducible preparation of working solutions for standards, improving consistency across experiments that rely on fluorescence intensity comparisons.
4. Peptide Conjugation Intermediates
Abz-Gly-OH · HCl is also used as a functional amino acid derivative in peptide conjugation and labeling strategies where an Abz aromatic tag is required as a reporter group. Chemical biology laboratories incorporate Abz-Gly units into larger constructs to create fluorescently traceable peptide reagents for studying processing, binding, or trafficking in controlled experimental systems. The combination of a reactive amino acid framework with the Abz chromophore enables downstream coupling into peptide scaffolds while maintaining a reliable fluorescence signature for tracking the resulting conjugates.
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