Bz-Asn-pNA is a benzoyl-protected asparagine derivative bearing a p-nitroanilide (pNA) leaving group, classed as an amino acid amide substrate rather than a free amino acid. The molecule contains an asparagine side chain with a primary amide, a benzoyl (Bz) protecting group on the amino functionality, and a carboxamide linked to the p-nitroanilide chromophore, providing a defined electrophilic amide site for controlled cleavage assays. In biochemical and analytical workflows, it is used as a substrate analog to monitor amide bond hydrolysis or protease-like activity by tracking the release or signal change associated with the p-nitroaniline moiety, supporting enzyme-substrate studies and method development for peptide-processing enzymes.
CAT No: CP26723
CAS No:201733-11-1
Synonyms/Alias:Nalpha-Benzoyl-L-asparagine4-nitroanilide;201733-11-1;Bz-Asn-pNA;AC1OLRGH;SCHEMBL5341361;CTK8E9450;ZINC4899705;RT-014646;(2S)-2-benzamido-N-(4-nitrophenyl)butanediamide
Bz-Asn-pNA is the benzoyl-protected asparagine derivative bearing a p-nitroanilide (pNA) leaving group, combining an N-benzoyl amide-protected amino acid backbone with a chromogenic anilide functionality. The molecule contains a stereodefined asparagine core with a side-chain amide (-CH2-CONH2) that can participate in hydrogen bonding and selective derivatization logic during peptide and amide chemistry. The p-nitroanilide moiety enables spectrophotometric readout upon enzymatic or chemical cleavage, while the benzoyl group modulates nucleophilicity at the amino nitrogen and supports controlled coupling/deprotection strategies. As a compact, chiral amino acid-based substrate analog, Bz-Asn-pNA functions as an intermediate for assay development and as a reagent platform for downstream synthesis of asparagine-containing peptidic and peptidomimetic structures.
1. Enzyme Assay Substrates
Bz-Asn-pNA is used in biochemical research as a chromogenic substrate for protease and peptidase activity profiling, where the p-nitroanilide group generates a measurable signal upon cleavage. The N-benzoyl protection and the asparagine side-chain amide help define substrate recognition by maintaining amide-rich hydrogen-bonding patterns that enzymes often require for specificity. The defined amino acid geometry supports mechanistic studies of cleavage preferences at the Asn position, enabling structure-function comparisons across related amino acid derivatives. The resulting assay workflow supports inhibitor screening libraries and method development for analytical research focused on amino acid sequence selectivity.
2. Peptide Coupling Building Block
Bz-Asn-pNA is applied in synthetic organic chemistry and peptide chemistry as an asparagine-derived intermediate whose protected nitrogen and amide functionalities can be leveraged for controlled transformations. The benzoyl-protected amino group can be retained during specific coupling steps or removed under established deprotection schemes to reveal an N-competent asparagine unit for further peptide bond formation. The side-chain carboxamide of the asparagine core can be used to generate additional hydrogen-bonding interactions in peptide analogs or to guide orthogonal protection planning for multi-step syntheses. Downstream conversion of the pNA-bearing amide into alternative leaving groups or end-functional handles can support the preparation of Asn-containing peptide building blocks and peptidomimetic linkers for research-grade scaffold construction.
3. Chiral Amino Acid Derivatization
Bz-Asn-pNA serves as a chiral amino acid intermediate for stereochemical studies and derivatization workflows where retention or transfer of stereochemical information matters. The stereogenic center in the asparagine backbone, combined with the N-benzoyl amide and side-chain carboxamide, provides a defined hydrogen-bonding and reactivity profile that can be exploited when designing protected amino acid derivatives. The p-nitroanilide group introduces a spectroscopic handle that can be used to monitor conversion, assess selectivity, or track cleavage events during synthetic route development. The compound can therefore be employed to generate stereochemically characterized Asn analogs for downstream peptide science, method validation, and fine chemical synthesis planning.
4. SAR And Protease Specificity Studies
Bz-Asn-pNA is utilized in drug discovery research programs focused on structure-activity relationship studies of protease recognition and substrate specificity. The Asn residue identity is encoded through the side-chain carboxamide, while the benzoyl-protected N-terminus constrains the local amide environment that influences binding and cleavage. The p-nitroanilide readout enables comparative evaluation of analogs that vary in protecting groups, leaving-group electronics, or side-chain substitution patterns. Data generated from such substrate analog panels can support molecular design iterations for peptidomimetics and inhibitor candidates that target sequence-selective proteolysis.
5. Analytical Research Standards
Bz-Asn-pNA can be applied in analytical research as a reference substrate and chromatographic/spectroscopic standard for monitoring enzymatic cleavage and for validating assay conditions. The presence of the p-nitroanilide chromophore provides a direct optical reporting element, while the benzoyl-protected asparagine framework supports consistent fragmentation behavior under cleavage assays. The defined functional group set, including the side-chain carboxamide and multiple amide bonds, supports reproducible retention characteristics and peak assignment in method development for amino acid derivative analytics. The compound can also serve as a starting material for preparing related standards that map cleavage specificity across Asn-containing motifs in biochemical testing workflows.
6. Fine Chemical And Intermediate Manufacture
Bz-Asn-pNA is relevant to process chemistry and specialty chemical production as a measurable, well-defined amino acid derivative that can be manufactured and used as an intermediate in multi-step synthesis. The N-benzoyl protection strategy enables controlled handling of the amino functionality during manufacturing, while the pNA amide provides a stable, isolable product form suited to downstream conversion into related protected amino acid derivatives. The asparagine side-chain amide supports predictable derivatization logic for generating Asn-containing building blocks used in peptide construction and peptidomimetic assembly. The compound's structure aligns with industrial intermediate preparation needs where standardized, assay-compatible amino acid substrates and chiral derivative platforms are required for consistent downstream synthetic and analytical operations.
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