H-Val-pNA · HCl is a hydrochloride salt of the valine-derived p-nitroanilide (pNA) amino acid derivative, featuring the valine side chain attached to a carboxamide linked to a p-nitroaniline reporter group. The molecule contains an amide functional group and a p-nitroaniline chromophore, with the "· HCl" indicating protonation of a basic site to form a salt form suitable for handling. In biochemical and analytical workflows, this derivative is used as a substrate analogue in enzyme activity assays and as a chromogenic/absorptive reporter system for monitoring cleavage events that release the p-nitroaniline moiety.
CAT No: CP27468
CAS No:77835-49-5
Synonyms/Alias:77835-49-5;L-Valinep-nitroanilidehydrochloride;H-Val-PnaHCl;(S)-2-Amino-3-methyl-N-(4-nitrophenyl)butanamidehydrochloride;L-Valine4-nitroanilidehydrochloride;H-VAL-PNAHCL;C11H15N3O3.HCl;V6005_SIGMA;CTK8G0688;7260AH;KM1879;MFCD00058470;AKOS022186112;AK144168;ST24035996
H-Val-pNA · HCl is a hydrochloride salt of the valine-derived p-nitroanilide, featuring an L-valine stereocenter linked through an amide to p-nitroaniline (pNA) and bearing a free amino acid functionality as part of the salt form. The p-nitroanilide chromophore provides a measurable UV-Vis signal upon enzymatic or chemical cleavage, while the valine side chain (isopropyl) supports substrate recognition by proteases that prefer hydrophobic residues. The HCl counterion improves handling and can influence solubility and reaction conditions for peptide coupling or assay workflows. The compound therefore functions as a chiral amino acid-based analytical and intermediate reagent in amino acid chemistry, peptide science, and enzyme-focused synthetic studies.
1. Protease Activity Assays
H-Val-pNA · HCl is applied in biochemical assay development for protease activity profiling, where the p-nitroanilide moiety acts as a chromogenic leaving group. The amide linkage between the valine residue and pNA enables cleavage pathways that translate substrate turnover into a quantifiable absorbance change. The L-valine stereochemistry and hydrophobic side chain can be matched to protease specificities for branched-chain amino acid substrates, supporting structure-function studies of enzyme selectivity. The resulting readout enables downstream comparison of inhibitor panels, substrate analogs, and reaction-condition effects in enzyme research and screening workflows.
2. Peptide Coupling Intermediate
H-Val-pNA · HCl is suitable for synthetic organic chemistry routes that require a valine-derived amide intermediate bearing a chromogenic handle. The amino acid backbone in salt form can be leveraged for controlled derivatization strategies, including conversion to protected forms or activation for coupling to carboxylic acid partners when building peptide-like structures. The pNA group can serve as a reporter functionality during method development, allowing monitoring of coupling efficiency or cleavage behavior in peptide chemistry contexts. The compound thus supports protected amino acid synthesis planning and intermediate preparation for fine chemical manufacturing where amino acid-derived amides are required.
3. Chiral Substrate Design
H-Val-pNA · HCl is used in chemical biology and enzyme studies focused on chiral substrate design and stereochemical control. The defined L-valine configuration provides a stereochemically consistent handle for probing how proteases and peptidyl transfer systems recognize amino acid geometry and side-chain hydrophobicity. The p-nitroanilide reporter allows rapid readout of cleavage events, enabling iterative design of valine-containing analogs with altered sterics or electronics. The compound can be employed as a reference substrate in SAR studies of substrate preferences, supporting rational selection of amino acid building blocks for peptide analog construction.
4. Analytical Reference Standard
H-Val-pNA · HCl is applied as an analytical research standard in method validation for chromogenic peptide substrates and amino acid-based assay components. The stable hydrochloride salt form supports reproducible preparation of assay solutions and consistent chromophore response under defined conditions. The distinct pNA chromophore enables straightforward detection by UV-Vis, supporting calibration and traceable quantification in enzyme kinetics experiments. The compound's structure also makes it suitable for characterizing related valine amide derivatives during synthetic workup and impurity tracking in peptide chemistry and industrial intermediate development.
5. Industrial Enzyme Screening
H-Val-pNA · HCl can be employed in industrial process chemistry contexts where protease activity monitoring is required during biocatalysis development or substrate processing optimization. The valine-pNA architecture provides a direct, chromogenic measure of cleavage that can be adapted to high-throughput screening of enzyme variants and process conditions. The salt form supports practical handling in manufacturing-adjacent workflows that require consistent reagent solubility and assay reproducibility. The compound therefore functions as a process-relevant amino acid derivative for evaluating enzyme performance and guiding selection of downstream synthetic conditions in specialty chemical production.
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