Nps-Phe-OH · DCHA is a phenylalanine-derived amino acid derivative presented as a dicyclohexylamine (DCHA) salt, featuring a substituted aromatic side chain characteristic of phenylalanine. The molecule contains a free carboxylic acid (-COOH) and an amino acid backbone with an Nps (p-nitrophenylsulfenyl)-type sulfenamide/activated N-substitution indicated by "Nps," which modulates the reactivity of the amino functionality relative to the corresponding unprotected amino acid. In peptide and amino acid chemistry workflows, the salt form and Nps substitution support controlled handling and stepwise incorporation into protected or activated peptide-building sequences, while the aromatic Nps group can be used as a structural handle for analytical characterization of the derivative during synthesis and purification.
CAT No: CP26925
CAS No:2688-22-4
Synonyms/Alias:(2S)-2-{[(2-nitrophenyl)sulfanyl]amino}-3-phenylpropanoicacid;dicha;2688-22-4;NPS-PHE-OHDCHA;Nps-Phe-OH.DCHA;AM033409
Nps-Phe-OH · DCHA is a chiral, Nps-protected phenylalanine derivative presented as a DCHA salt, where the phenylalanine backbone bears a free carboxylic acid (-CO2H) and an N-(Nps) protecting group that modulates amine reactivity during peptide coupling. The stereogenic center of the phenylalanine residue is retained, enabling stereochemically defined incorporation into peptide sequences and amino acid modification workflows. The Nps group provides controlled N-deprotection behavior under peptide synthesis conditions, while the carboxylic acid supports activation to form acylating intermediates for amide bond formation. The DCHA counterion improves handling characteristics for synthetic workup and downstream intermediate preparation, while the aromatic side chain remains available for conjugation, derivatization, or incorporation into structure-directed molecular scaffolds.
1. Peptide Coupling Chemistry
Nps-Phe-OH · DCHA is applied in peptide synthesis and protected amino acid chemistry as an Nps-protected phenylalanine building block with a carboxylic acid handle for coupling. The combination of an N-protected amine and a free acid enables standard peptide coupling strategies to generate amide bonds while suppressing undesired side reactions from the amino nitrogen. The preserved stereochemistry at the phenylalanine center supports stereodefined peptide chain assembly, and the aromatic side chain can be used as a recognition element in peptide analogs. The DCHA salt form can be leveraged to support reproducible solid-state handling and consistent dosing in fine chemical synthesis of peptide intermediates.
2. Unnatural Amino Acid Incorporation
Nps-Phe-OH · DCHA serves as a chiral amino acid intermediate for incorporating phenylalanine residues into unnatural or engineered peptide frameworks where controlled N-protection is required. The Nps-protected amine allows sequential assembly of peptide segments without premature N-reactivity, while the free carboxyl group supports selective activation for C-terminal or internal residue formation. The phenyl side chain can participate in aromatic stacking motifs that influence conformational preferences in peptidomimetics and sequence-defined molecular scaffolds. Downstream derivatization can be performed after peptide assembly by converting the aromatic ring into functionalized analogs or by using the residue as a platform for SAR-driven library construction.
3. Side-Chain Functionalization
Nps-Phe-OH · DCHA is utilized in synthetic organic chemistry and amino acid derivatization workflows that target aromatic side-chain modification while maintaining peptide-compatible functionality. The phenylalanine aromatic ring provides a chemically accessible site for electrophilic substitution, oxidative transformation, or cross-coupling-based elaboration after the protected amino acid has been incorporated into a peptide or held as an intermediate. The Nps protection strategy supports chemoselective manipulation of the side chain by reducing interference from the amino group during side-chain functional group installation. The resulting functionalized phenylalanine-containing intermediates can then be carried forward into peptidomimetic construction, chemical biology probes, or structure-directed scaffold generation.
4. Analytical Research Standards
Nps-Phe-OH · DCHA is suitable for analytical research and method development as a stereodefined, protected amino acid reference material for monitoring peptide coupling and deprotection steps. The defined Nps protection pattern and the free carboxylic acid enable chromatographic and mass spectrometric discrimination from unprotected phenylalanine and from alternative protecting-group isomers. The DCHA salt form can support consistent sample preparation behavior for LC-MS or HPLC workflows used to track protected amino acid consumption and intermediate formation. The compound can also function as a structural standard when validating analytical methods for peptide building block identity, stability, and impurity profiling in amino acid derivative manufacturing.
5. Pharmaceutical Intermediate Preparation
Nps-Phe-OH · DCHA is relevant to pharmaceutical manufacturing and process chemistry as a protected amino acid intermediate for producing peptide-based or peptide-containing drug candidates and related process intermediates. The Nps-protected amine and free carboxylic acid support controlled conversion into acylating species for amide bond formation under manufacturing-compatible coupling conditions. The stereochemical integrity of the phenylalanine residue supports downstream consistency in sequence-defined intermediates where stereochemical purity is critical for reproducible synthesis. The salt form with DCHA can be incorporated into batch processing workflows to improve handling, weighing accuracy, and reproducibility of intermediate preparation for fine chemical production.
6. Bioconjugation and Chemical Biology
Nps-Phe-OH · DCHA can be employed in chemical biology workflows that require phenylalanine-containing conjugation handles within peptide or peptidomimetic constructs. The protected amino acid structure supports stepwise assembly of conjugatable peptide fragments where the Nps group can be removed or transformed according to the chosen peptide strategy, while the aromatic phenylalanine residue can contribute to molecular recognition or serve as a scaffold for later functionalization. The free carboxyl functionality enables integration into amide-linked bioconjugates, including linker-bearing peptide segments used for target-binding or assay development. The compound thus functions as a chiral, peptide-compatible intermediate bridging amino acid derivatization chemistry with biomolecule modification and applied biochemical research.
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