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Cité dans 0 publications à comité de lecture couvrant la chromatographie, la synthèse organique et les réactions de couplage croisé.

Spécifications

Synonymes

Spécifications et pureté

powder

Conditions de stockage de stockage

Store at -20°C

Expédié en

Ice chest + Ice pads

Ce produit nécessite l'expédition en chaîne froide. Les services terrestres et autres services économiques ne sont pas disponibles.

Noms et identifiants

Sourires canoniques

C1=CC=C2C=C(C=CC2=C1)NC(=O)C(CC3=CN=CN3)N

IUPAC Name

(2S)-2-amino-3-(1H-imidazol-5-yl)-N-naphthalen-2-ylpropanamide

InChIKey

DKDILZBBFKZMRO-HNNXBMFYSA-N

INCHI

1S/C16H16N4O/c17-15(8-14-9-18-10-19-14)16(21)20-13-6-5-11-3-1-2-4-12(11)7-13/h1-7,9-10,15H,8,17H2,(H,18,19)(H,20,21)/t15-/m0/s1

Isomères SMILES

C1=CC=C2C=C(C=CC2=C1)NC(=O)[C@H](CC3=CN=CN3)N

Poids moléculaire

280.32

Reaxy-Rn

44307826

Reaxys-RN_link_address

https://www.reaxys.com/reaxys/secured/hopinto.do?context=S&query=IDE.XRN=44307826&ln=

Documentation

📋 Fiche de données de sécurité (FDS)

Document complet couvrant les dangers, la manipulation, le stockage et la conformité réglementaire.

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✅ Certificat d'analyse (COA)

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Données avancées

Taxonomic Classification

Taxonomy Tree

Kingdom Organic compounds
- Superclass Organic acids and derivatives
  - Classe Carboxylic acids and derivatives
    - Subclass Amino acids, peptides, and analogues
      - Level5 Amino acids and derivatives
        Level6 Alpha amino acids and derivatives
        Level7 Histidine and derivatives

Kingdom	Organic compounds
Superclass	Organic acids and derivatives
Classe	Carboxylic acids and derivatives
Subclass	Amino acids, peptides, and analogues
Intermediate Tree Nodes	Amino acids and derivatives - Alpha amino acids and derivatives
Direct Parent	Histidine and derivatives
Alternative Parents	Alpha amino acid amides Naphthalenes N-arylamides Aralkylamines Fatty amides Imidazoles Heteroaromatic compounds Secondary carboxylic acid amides Azacyclic compounds Organopnictogen compounds Organic oxides Monoalkylamines Hydrocarbon derivatives Carbonyl compounds
Molecular Framework	Aromatic heteropolycyclic compounds
Substituents	Histidine or derivatives - Alpha-amino acid amide - Naphthalene - N-arylamide - Aralkylamine - Fatty amide - Fatty acyl - Benzenoid - Azole - Imidazole - Heteroaromatic compound - Carboxamide group - Secondary carboxylic acid amide - Azacycle - Organoheterocyclic compound - Amine - Primary amine - Organooxygen compound - Organonitrogen compound - Hydrocarbon derivative - Primary aliphatic amine - Organic oxide - Organopnictogen compound - Organic nitrogen compound - Carbonyl group - Organic oxygen compound - Aromatic heteropolycyclic compound
Description	This compound belongs to the class of organic compounds known as histidine and derivatives. These are compounds containing cysteine or a derivative thereof resulting from reaction of cysteine at the amino group or the carboxy group, or from the replacement of any hydrogen of glycine by a heteroatom.
External Descriptors	Not available
1. Djoumbou Feunang Y, Eisner R, Knox C, Chepelev L, Hastings J, Owen G, Fahy E, Steinbeck C, Subramanian S, Bolton E, Greiner R, and Wishart DS. ClassyFire: Automated Chemical Classification With A Comprehensive, Computable Taxonomy. Journal of Cheminformatics, 2016, 8:61. DOI: 10.1186/s13321-016-0174-y

Structure 3D

Cibles associées (humaines)

KDM4A Tchem Lysine-specific demethylase 4A (52245 Activities)

Discover Target: KDM4A

Activity Type	Relation	Activity value	Units	Action Type	Journal	PubMed Id	doi	Assay Aladdin ID

EYA2 Tbio Eyes absent homolog 2 (5884 Activities)

Discover Target: EYA2

Activity Type	Relation	Activity value	Units	Action Type	Journal	PubMed Id	doi	Assay Aladdin ID

Mécanismes d'action

Certificats (CoA, COO, BSE/TSE et tableau d'analyse)

C of A & Other Certificates(BSE/TSE, COO):

Analytical Chart:

Propriétés chimiques et physiques

Poids moléculaire	280.320 g/mol
XLogP3	1.600
Hydrogen Bond Donor Count	3
Hydrogen Bond Acceptor Count	3
Rotatable Bond Count	4
Exact Mass	280.132 Da
Monoisotopic Mass	280.132 Da
Topological Polar Surface Area	83.800 Å²
Heavy Atom Count	21
Formal Charge	0
Complexity	362.000
Isotope Atom Count	0
Defined Atom Stereocenter Count	1
Undefined Atom Stereocenter Count	0
Defined Bond Stereocenter Count	0
Undefined Bond Stereocenter Count	0
The total count of all stereochemical bonds	0
Covalently-Bonded Unit Count	1

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Application Protocols

Tested applications, recommended dilutions, and in‑house protocols were not provided for this SKU.

Not specified for this item; refer to CoA/Spec Sheet.
For general assay setup guidance, see the “Reaction Conditions” tab, and consult enzyme‑specific literature for validated protocols and readout parameters.

Biological Roles

This compound is a synthetic substrate and does not have a natural biological role. Its utility stems from mimicking an N‑terminal histidine residue coupled to a fluorogenic/ chromogenic leaving group.

Enzymatic context (literature):
- Aminopeptidases and related exopeptidases may recognize L‑histidine at the N‑terminus; hydrolysis of the arylamide bond liberates β‑naphthylamine for detection.
- Suitable for probing substrate preference for histidine versus other residues (e.g., Leu‑βNA, Arg‑βNA).
Kinetic/biophysical considerations (general):
- The imidazole side chain (pKa ~6.0, literature) can influence binding and turnover depending on assay pH and active‑site environment.
- Fluorometric detection of the released β‑naphthylamine enables sensitive quantification of enzyme activity in complex biological samples after appropriate sample cleanup.
Experimental roles:
- Tool compound for enzyme characterization, inhibitor screening, and activity staining in gels (post‑electrophoresis coupling to diazonium dyes).

No medical or clinical claims are made. Use is restricted to laboratory research applications.

Buffer Applications

This product is not a buffering agent and is not typically used to prepare buffer systems.

Practical note (assay context, literature): For enzyme assays using L‑histidine β‑naphthylamide, common buffers include Tris‑HCl, HEPES, or phosphate at pH 7.0–8.0. Ionic strength (50–150 mM) and additives (e.g., 0.01% nonionic surfactant, 0.5–2 mM metal ions or chelators as appropriate) should be optimized for the target enzyme.

For actual buffer formulation details and compatibility with your enzyme system, consult primary literature and validate empirically.

Green Alternatives

While the molecule itself is the functional substrate, greener choices often relate to solvent and assay media.

Opportunity areas:
- Reduce or replace dipolar aprotic solvents (DMSO/DMF) where feasible.
- Favor aqueous buffers and benign co‑solvents while preserving solubility and enzyme activity.
Comparison (literature‑based, general):

| Aspect | Conventional choice | Greener alternative | Trade‑offs | |---|---|---|---| | Stock solvent | DMSO | Aqueous acidic stock (e.g., 0.05–0.1 M HCl), or ethanol ≤10% | Aqueous acid requires rapid neutralization; EtOH may affect some enzymes | | Co‑solvent in assay | 1–2% DMSO | ≤1% ethanol, glycerol (1–5%), or PEG‑400 (≤1%) | Viscosity and potential interference with kinetics | | Waste handling | Organic/halogenated mixes | Segregate minimal DMSO aqueous waste | Requires procedural discipline |

Practical guidance:
- Pilot solubility in slightly acidic aqueous media to reduce DMSO usage.
- Use minimal co‑solvent compatible with enzyme performance; run solvent controls.
- Prepare smaller, single‑use aliquots to limit freeze‑thaw and reduce discarded residues.

Pharmaceutical Uses

Not used as a pharmaceutical active ingredient or common excipient. This substrate is intended for laboratory research applications such as enzymology assays and analytical method development.

Regulatory status: No pharmacopeial monograph is known for L‑histidine β‑naphthylamide (literature search context). Any use in GMP/GLP workflows would require internal qualification and method validation.
Relevance to pharma R&D (general):
- Tool compound for characterizing peptidase activity in biological matrices.
- Screening substrate in hit‑to‑lead enzymology platforms, with caution to avoid cross‑reactivity and to confirm mechanism using orthogonal substrates.

No therapeutic or clinical claims are made.

Physical Properties

Item-specific specifications have not been provided for this SKU. The following values are general/literature guidance for the neutral free base and should be verified against the CoA/Spec Sheet before use in regulated methods.

Appearance: Not specified for this item; refer to CoA/Spec Sheet.
Molecular weight: ~280.33 g/mol (literature/computed for C16H16N4O).
Molecular formula: C16H16N4O (literature/computed).
Melting point: Frequently reported for amino acid β‑naphthylamides as solid organics with decomposition; specific MP for L‑histidine β‑naphthylamide is not well established in primary sources. Not specified for this item; refer to CoA/Spec Sheet.
Solubility (literature/typical):
- Water: Low to sparingly soluble at neutral pH due to hydrophobic naphthyl group; solubility increases in mildly acidic aqueous media (e.g., 0.1 M HCl) or with co‑solvents (DMSO, DMF).
- Organic: Soluble in polar aprotic solvents (DMSO, DMF); limited in alcohols; poor in nonpolar hydrocarbons.
pKa (literature/estimated qualitative):
- Imidazole side chain pKa ~6.0 (histidine motif, literature); overall compound displays multiple acid/base sites; exact macroscopic pKa values for the arylamide are not well documented.
LogP/logD (qualitative literature expectation): Amphipathic; higher hydrophobicity than free histidine due to β‑naphthyl; logD is pH‑dependent.
UV/Vis (literature/typical): Naphthyl chromophore shows absorbance in the near‑UV (approx. 220–280 nm); upon enzymatic release of β‑naphthylamine, fluorescence is observed (Ex ~330–340 nm, Em ~410 nm, literature).
Density, refractive index: Not applicable/typically unreported for solids; Not specified for this item; refer to CoA/Spec Sheet.

Quality and Grades

Grade/Purity (item-specific): Not specified for this item; refer to CoA/Spec Sheet.
What “research use only” means: Supplied for laboratory research and analytical applications; not intended for human or animal therapeutic or diagnostic use.
Typical quality considerations for amino acid β‑naphthylamides (general):
- Chemical identity: Confirmed by NMR and MS; chiral integrity at the α‑center (L‑configuration) should be verified (e.g., chiral HPLC or optical rotation).
- Chromatic purity: Key to low background in fluorometric/colourimetric enzyme assays; impurities can elevate baseline absorbance/fluorescence.
- Residual solvents: Important if using sensitive enzymes; verify by GC‑headspace if needed.
- Water content: Can impact dissolution and stability in DMSO; Karl Fischer titration may be used as needed.
Stabilizers/additives: Not specified for this item; refer to CoA/Spec Sheet. In general, neat solids are provided without stabilizers; if a salt form is provided, counter‑ions will be listed on the CoA.
Documentation: Request batch CoA for exact purity, identity tests, residual solvents, optical rotation, and assay suitability if your workflow is quantitative (e.g., kinetic enzyme assays).

Reaction and Applications

Primary application is as a chromogenic/fluorogenic enzymology substrate. Aminopeptidases that specifically remove N‑terminal L‑histidine from peptides can hydrolyze L‑histidine β‑naphthylamide to release β‑naphthylamine, which is detectable colorimetrically (via diazotization coupling) or fluorometrically.

Enzymology (literature):
- Substrate class: X‑β‑naphthylamides (X = amino acid) for profiling aminopeptidase specificity and activity.
- Readout modes:
  - Fluorescence of β‑naphthylamine: Ex ~330–340 nm, Em ~410 nm.
  - Color development: Coupling β‑naphthylamine with diazonium salts (e.g., Fast Garnet GBC, Fast Blue) to form azo dyes measured at visible wavelengths.
- Use cases: Enzyme kinetics (Km, kcat), inhibitor screening, specificity mapping for histidine‑preferring aminopeptidases.
Practical tips:
- Ensure substrate purity to minimize background fluorescence. Include a no‑enzyme control.
- Maintain consistent DMSO content across wells when using organic stocks.
- For end‑point azo dye assays, strictly control coupling reagent concentration, pH (often ~6–8), and time to ensure linear response.
Related chemistries (general): Arylamide hydrolysis by proteases/peptidases; the imidazole side chain can influence binding/turnover relative to aliphatic substrates.

Note: Specific enzyme compatibilities and kinetics vary by source and assay conditions; consult primary literature and validate in your system.

Reaction Conditions

Guidance below summarizes common assay conditions from the enzymology literature; optimize for your specific enzyme and matrix. These are not item‑specific specifications.

Stock solutions:
- Dissolve in DMSO at 10–50 mM; store aliquots at −20°C, protected from light.
- Alternatively, prepare an acidic aqueous stock (e.g., 10–20 mM in 0.05–0.1 M HCl) immediately before use.
Assay buffer (examples):
- 50 mM Tris‑HCl, pH 7.5–8.0, 100 mM NaCl; optional 0.01% Tween‑20.
- 50 mM HEPES, pH 7.4, with Mg2+ or Zn2+ if required by the enzyme; or include EDTA if metal chelation is needed (enzyme dependent).
Substrate concentration: 10–500 μM typical screening range; for kinetics, use 0.1–5× estimated Km.
Temperature: 25–37°C.
Detection:
- Fluorescence (β‑naphthylamine): Ex 330–340 nm / Em ~410 nm. Calibrate with authentic β‑naphthylamine standards for quantitation.
- Colorimetric coupling: Add diazonium salt (e.g., Fast Garnet GBC) post‑hydrolysis; measure at visible λmax per coupling reagent supplier instructions.
Controls: No‑enzyme, no‑substrate, and solvent controls; include a known inhibitor/activator where applicable.
Data quality: Maintain constant solvent content across wells; verify linearity with respect to time and enzyme concentration; minimize inner‑filter effects at higher substrate/product absorbance.

Always validate conditions with your specific enzyme preparation.

Safety and Handling

Product-specific GHS details were not provided. Always consult the SDS for authoritative safety information.

GHS/Classification (item-specific): Not specified for this item; refer to SDS.
General hazards (chemistry knowledge): Aromatic amide containing a naphthyl moiety; may cause irritation to eyes, skin, and respiratory tract. Avoid dust generation. The released β‑naphthylamine in enzymatic assays is a separate chemical with its own hazards—handle downstream products accordingly.
PPE recommendations (good laboratory practice):
- Wear lab coat, safety glasses, and appropriate chemical-resistant gloves (e.g., nitrile).
- Use in a fume hood when weighing or preparing concentrated stock solutions, especially in organic solvents (DMSO, DMF).
Handling tips:
- Minimize exposure to light to protect the naphthyl chromophore from photodegradation.
- Prepare fresh solutions when possible; avoid prolonged storage of aqueous stocks at ambient temperature.
Incompatibilities (general): Strong oxidizers; strong acids/bases may promote degradation or racemization under forcing conditions.
First-aid overview (consult SDS for details):
- Eye/skin contact: Rinse with water for at least 15 minutes; remove contaminated clothing.
- Inhalation: Move to fresh air; seek medical attention if symptoms persist.
- Ingestion: Rinse mouth; do not induce vomiting; seek medical attention.
Waste: Collect organic solvent solutions and fluorescent assay waste in labeled hazardous waste containers. Follow institutional and local regulations.

Solvent Selection

L‑Histidine β‑naphthylamide is an amphipathic solid: a polar amino acid headgroup and a hydrophobic β‑naphthyl tail. This duality drives practical solvent choices for stock solutions and assay buffers.

Polarity and miscibility (literature/typical):
- Readily soluble in polar aprotic solvents (DMSO, DMF) at 10–100 mM.
- Sparingly soluble in pure water at neutral pH; solubility improves in mildly acidic aqueous media (e.g., 10–100 mM HCl) or with 5–20% co‑solvent (DMSO).
- Poorly soluble in nonpolar solvents (hexanes, toluene).
Recommended practices (general):
- Prepare a concentrated DMSO stock (e.g., 10–50 mM), then dilute into buffered aqueous media to reach final DMSO ≤1–2% v/v for enzyme assays.
- If DMSO is undesirable, dissolve in minimal DMF, or create an acidic aqueous concentrate (e.g., pH 3–4) followed by neutralization in buffer immediately before use.
Buffer compatibility (assay context): Tris, HEPES, or phosphate buffers at pH 7.0–8.0 are commonly used for aminopeptidase assays; include 0.01–0.1% nonionic surfactant if adsorption is observed.
Comparison (literature‑based):
- DMSO: highest solvency; excellent for freezer‑stable aliquots; potential enzyme inhibition at >2%.
- DMF: similar solvency; more hygroscopic/odor; consider toxicity.
- Aqueous acid (e.g., 0.1 M HCl): improves dissolution without organic co‑solvents; requires prompt pH adjustment on dilution.

Storage and Reconstitution

Storage (item-specific): Store at −20°C (Product Data). Shipments are supplied cold (ice chest + ice pads) to preserve stability.
Light/moisture: As a precaution, protect from light and store desiccated; return to cold promptly after use. These are general best practices for arylamide fluorogenic substrates; specific stability data are Not specified for this item; refer to CoA/Spec Sheet.
Reconstitution (general/literature guidance):
- Prepare concentrated stocks in anhydrous DMSO (e.g., 10–50 mM). Vortex and, if needed, sonicate briefly to aid dissolution.
- Alternatively, dissolve freshly in mildly acidic aqueous solution (e.g., 0.05–0.1 M HCl) and dilute into assay buffer immediately, adjusting pH to the working range.
- Filter sterilize (0.22 μm) if sterility is required for cell‑free assays; avoid extended filtration times that may cause adsorption losses.
Aliquoting: Dispense single‑use aliquots to avoid repeated freeze–thaw. Keep DMSO stocks at −20°C in amber vials.
Stability: Long‑term stability, exact shelf life, and freeze–thaw tolerance are Not specified for this item; refer to CoA/Spec Sheet. As general practice, monitor background signal and product formation standards to verify performance over time.

Research Use Only: For laboratory research use; not for diagnostic or therapeutic applications.

Structure and Identity

L‑Histidine β‑naphthylamide is an amino acid–arylamide conjugate in which the L‑histidine carboxyl group is amidated by β‑naphthylamine, leaving the α‑amine and imidazole side chain of histidine intact.

Item-specific identifiers (Product Data):
- CAS: 7424-15-9
- CID: 688489
- InChIKey: 65577 (as provided)
- SMILES: Not specified for this item; refer to CoA/Spec Sheet.
Structural description (general/literature):
- Core features: α‑amino acid backbone (L‑configuration), imidazole side chain (histidine), and an amide linkage to a β‑naphthyl group (1‑naphthylamine derived).
- 2D structure in words: An L‑histidine residue with free α‑NH2 and imidazole ring; the α‑carboxyl is converted to a CONH–β‑naphthyl moiety. The aromatic domain is a fused bicyclic naphthalene attached via –NH– to the carbonyl carbon of the histidine carboxamide.
- Stereochemistry: One stereocenter at the α‑carbon in the L‑configuration (S absolute configuration by the Cahn–Ingold–Prelog convention for L‑histidine, literature).
Empirical formula and molecular weight (computed/literature for the neutral free base):
- Molecular formula: C16H16N4O (literature/computed from L‑His + β‑naphthylamine − H2O)
- Molecular weight: ~280.33 g/mol (literature/computed)

Notes:

If a different salt form (e.g., hydrochloride) applies, formula/MW will differ; verify on the CoA/Spec Sheet for this specific SKU.

Synthetic Utility

As a designed arylamide substrate, L‑histidine β‑naphthylamide is not commonly used as a general synthetic building block. However, its structural features inform synthesis and modification strategies.

Functional group highlights (general):
- Secondary arylamide (–CONH–Ar) linking the histidine carboxyl to β‑naphthylamine.
- Free α‑amine and imidazole side chain provide ionizable sites and potential derivatization handles.
Typical transformations (literature):
- Protection/deprotection: α‑NH2 (Boc, Fmoc) and imidazole (Trt) if further peptide elaboration or probe installation is desired.
- Labeling: Introduction of reporter tags (e.g., fluorophores, biotin) on the α‑amine enables bifunctional probes retaining the β‑naphthylamide leaving group for dual readouts.
- Salt formation: Acid addition salts (e.g., HCl) can enhance aqueous solubility for handling.
Synthesis overview (literature): Coupling of protected L‑histidine (free carboxyl) to β‑naphthylamine using carbodiimide (e.g., EDC/HOBt) or uronium reagents (HATU) under mild conditions, followed by deprotection and purification.

For routine lab use, this compound is primarily valued as an assay substrate rather than as a precursor in multistep syntheses.

Target Specificity

Item-specific biological target details (e.g., particular enzyme selectivity, tested reactivity) were not provided for this SKU.

Not specified for this item; refer to CoA/Spec Sheet and primary literature.
General note (literature): X‑β‑naphthylamide substrates are often used to probe aminopeptidase preferences; however, specificity and turnover vary widely among enzyme families and species. Empirical validation is essential.

Foire aux questions

How should this product be stored?

Store at ?20 °C. Freezer storage is required to maintain the specified shelf life.

How is this product shipped?

This product ships in an insulated container with ice pads. Unpack on arrival and transfer it to the storage condition stated above.

What are the CAS number, molecular formula and molecular weight?

The CAS Number is 7424-15-9, the molecular formula is C16H16N4O, and the molecular weight is 280.32 g/mol. InChIKey DKDILZBBFKZMRO-HNNXBMFYSA-N.

What documentation is provided?

Available product documentation, including Certificates of Analysis (COA), Safety Data Sheets (SDS), and specification sheets, is shown in the product document area. Document availability and access follow the current site policy.

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