ACV Tripeptide TFA , CAS No.A1455672

CAS: A1455672 Cat. No.: A1455672 Formula: C₁₆H₂₆F₃N₃O₈S Molecular Weight: 477.45

Storage

Desiccated,Store at -80°C

Shipped In

Dry ice packs + Cold packs

Overview

ACV Tripeptide TFA is the TFA form of ACV Tripeptide. ACV Tripeptide TFA is a key biosynthetic precursor of penicillin and cephalosporins and is found in Penicillium chrysogenum and Acremonium chrysogenum. ACV Tripeptide TFA is synthesized by a large non-ribosomal peptide synthase called ACV synthase.

Specifications

Storage

Desiccated,Store at -80°C

Shipped In

Dry ice packs + Cold packs

This product requires cold chain shipping. Ground and other economy services are not available.

Names and Identifiers

Molecular Weight

477.45

Application Protocols

No validated, item-specific protocols are provided in the Product Data for this SKU. Refer to the primary literature for ACV substrate assays with isopenicillin N synthase (IPNS) and related pathway enzymes.

General guidance (literature/informational)

• Prepare a fresh aqueous stock under reducing conditions if required (e.g., add DTT/TCEP compatible with your assay).
• Set up enzymatic reactions with Fe(II), ascorbate, buffer near neutral pH, and IPNS; quench at defined time points and analyze by LC–MS.

Always adapt conditions to your specific system and consult peer-reviewed sources. This product is for research use only.

Biological Roles

Literature context: ACV (δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine) is the committed biosynthetic intermediate in the formation of β-lactam antibiotics in fungi and some bacteria.

• Pathway position

  • Produced by the nonribosomal peptide synthetase ACV synthetase (ACVS) from L-α-aminoadipate, L-cysteine, and L-valine (epimerized to D-Val during assembly).
  • Converted by isopenicillin N synthase (IPNS), an Fe(II)/O2-dependent oxidase, into isopenicillin N via oxidative cyclization that forms both the β-lactam and thiazolidine rings.

• Biochemical features

  • Stereochemical configuration (L-L-D) is crucial for IPNS recognition and catalysis.
  • The free cysteinyl thiol participates in downstream ring formation; its oxidation to disulfide compromises substrate activity.

• Research relevance

  • Serves as a reference substrate to dissect enzyme mechanisms, oxygen activation chemistry, radical intermediates, and to benchmark engineered pathway variants in heterologous hosts.
  • Utilized to calibrate LC–MS metabolite profiling for flux analysis in NRPS pathways.

Note: This product is for research use only. No clinical or therapeutic claims are made or implied.

Buffer Applications

This product is not a buffering reagent and does not constitute a defined buffer system. It is typically used as a substrate/standard in aqueous assay buffers.

• Practical notes (literature/general)
  • Choose neutral, metal-chelated buffers (e.g., HEPES or Tris with controlled Fe(II) where required) for enzymology, adding reducing agents (DTT/TCEP) to preserve thiol state when compatible.
  • Avoid strongly basic buffers that can degrade peptide bonds or promote β-elimination at cysteine.

For precise buffer recipes or pH ranges, consult assay-specific literature or your institutional SOPs.

Green Alternatives

Perspective: The compound itself is a peptide; “greenness” considerations revolve around counterion choice, solvent systems, and assay media.

• Counterion considerations (literature/general)

  • TFA salts: Facilitate purification and solubility but introduce persistent fluorinated anions; disposal must follow local regulations.
  • Alternatives: Acetate or formate salts reduce halogenated waste and can simplify lyophilization/removal.

• Solvent systems

  • Prefer aqueous buffers whenever possible. Avoid halogenated solvents. If organic modifiers are required (HPLC, sample prep), choose MeOH or EtOH over acetonitrile where performance allows.

• Comparison (general)

  • TFA vs Acetate Salt
    • Environmental impact: TFA generates fluorinated waste; acetate is biodegradable.
    • Assay compatibility: TFA may suppress MS signals via ion-pairing; acetate/formate are more MS-friendly.
    • Stability: TFA salts may offer slightly improved solid-state stability; acetate is typically sufficient for routine work.

• Process tips

  • Ion-exchange to acetate before large-scale aqueous work to reduce TFA load.
  • Employ minimal organic content in buffers; recycle solvents where feasible.
  • Use catalytic amounts of acids for HPLC mobile phases (e.g., 0.1% formic acid) to enhance MS compatibility and reduce TFA usage.

Pharmaceutical Uses

No excipient/formulation role is specified for this item. ACV tripeptide is used in research as a biosynthetic intermediate/substrate and analytical standard.

• Item-specific status

  • Pharmacopeial status: Not specified for this item; refer to CoA/Spec Sheet.

• Research/manufacturing context (literature/general)

  • Employed in process development studies and pathway engineering to evaluate β-lactam biosynthesis; not intended for inclusion in finished dosage forms.

This product is for research use only and is not for human or veterinary use.

Physical Properties

Item-specific values

• Molecular Weight: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular Formula: Not specified for this item; refer to CoA/Spec Sheet.
• Appearance: Not specified for this item; refer to CoA/Spec Sheet.

Literature/general properties for peptide TFA salts (informational only)

• State: Typically an off-white to white amorphous solid or lyophilizate (literature, varies with preparation).
• Melting point: Often decomposes before melting; discrete MP not routinely reported for small peptides (literature).
• Solubility: Peptide TFA salts are generally readily soluble in water and aqueous buffers; sparingly soluble in alcohols; insoluble in nonpolar solvents (literature). Free thiols may oxidize in air; degassed buffers can help maintain reduced state.
• pKa/ionization: Multiple ionizable groups; net charge depends strongly on pH (literature). TFA association can acidify aqueous solutions slightly.
• Hygroscopicity: Many peptide salts are hygroscopic; handle quickly in low-humidity conditions (literature).

Practical implications

• For quantitative work (e.g., enzyme kinetics), determine exact counterion content and residual moisture by referencing the CoA or by independent analysis (e.g., anhydrous correction, TFA assay).

Quality & Grades

Item-specific quality information

• Grade/Purity: Not specified for this item; refer to CoA/Spec Sheet.

General notes on peptide product quality (literature/general)

• Typical characterization: Peptides are commonly qualified by analytical HPLC purity (area %) and identity by high-resolution MS and, if needed, 1H NMR. Counterion content (e.g., TFA %) and residual water/solvent are often reported.
• Implications of TFA salt: TFA enhances solubility and stability during isolation, but residual TFA can affect biological assays (pH, ion-pairing) and mass balance. For stringent applications, consider exchanging TFA for acetate or chloride via ion-exchange or repeated lyophilization from volatile acids.
• Batch-to-batch consistency: Examine the CoA for peptide content on an anhydrous basis, residual solvents, TFA equivalence, and endotoxin/bioburden if relevant to your workflow (though this product is for research use only).

Recommendation

• For quantitative studies (enzyme kinetics, standards), normalize by exact peptide content using CoA data and, if necessary, perform salt correction in your calculations.

Reaction & Applications

Use context: ACV tripeptide (literature) is the native substrate for isopenicillin N synthase (IPNS), the Fe(II)/O2-dependent enzyme that cyclizes ACV to isopenicillin N, the core β-lactam structure.

• Enzymology/biochemistry (literature/general)

  • Substrate assays: Employed to study IPNS kinetics, mechanism, and oxygen activation. Typical components include Fe(II), O2, ascorbate, and reducing agents to maintain cysteine thiol.
  • NRPS research: Serves as a reference product to interrogate ACV synthetase (ACVS) product fidelity, stereochemistry (L-L-D), and alternative substrate tolerance.

• Synthetic/chemoenzymatic applications (literature)

  • Chemoenzymatic β-lactam formation: ACV is converted enzymatically to isopenicillin N, which can be diversified to penicillin/cephalosporin frameworks.
  • Analogs: Variant tripeptides (A(Cys)X) probe structure–activity relationships; ACV itself is the benchmark control.

• Analytical applications (general)

  • LC–MS standards: Used as a reference standard for pathway profiling in engineered microbes expressing ACVS/IPNS.
  • Spectroscopic monitoring: Thiol oxidation state can be tracked to ensure substrate integrity during assays.

• Practical tips

  • Maintain anaerobic or reducing conditions to prevent thiol oxidation (DTT/TCEP as compatible).
  • Prepare fresh solutions; store aliquots at −80 °C to minimize degradation.
  • Verify counterion/peptide content from CoA to calculate exact molar concentrations for kinetic studies.

Reaction Conditions

General guidance (literature; not item-specific specifications). For enzymatic conversion of ACV to isopenicillin N by IPNS:

• Typical assay solvent: Aqueous buffer near neutral pH (e.g., 50 mM HEPES, pH ~7.0–7.5) with controlled ionic strength.
• Cofactors/additives: Fe(II) salt (e.g., Fe(NH4)2(SO4)2), ascorbate as reductant, and sometimes DTT/TCEP to maintain the cysteinyl thiol; oxygen supplied from air or defined O2 mixtures.
• Temperature: Often conducted at 20–30 °C to balance activity and stability.
• Concentration ranges: Substrate in the low micromolar to millimolar range depending on enzyme concentration and kinetics reported in the literature.
• Atmosphere: Ambient air or controlled O2; avoid excess chelators unless required for metal homeostasis.
• Analytical readouts: LC–MS quantitation of ACV consumption and isopenicillin N formation; spectrophotometric coupled assays are also described.

Handling/controls

• Include negative controls lacking Fe(II) or enzyme to account for non-enzymatic loss/oxidation.
• Prepare fresh ACV solutions; filter (0.22 μm) if needed; minimize light and air exposure.

Note: Parameters vary with enzyme source, purity, and expression system. Consult primary literature for detailed kinetics and optimization.

Safety & Handling

Authoritative safety data should be taken from the product SDS.

Item-specific hazard data

• Signal Word: Not specified for this item; refer to SDS.
• H-Statements: Not specified for this item; refer to SDS.
• GHS Classification: Not specified for this item; refer to SDS.
• Pictograms: Not specified for this item; refer to SDS.

General guidance for peptide/TFA salts (literature/general)

• Expected hazards: Low volatility; dust may cause mechanical irritation. TFA counterion can render solutions mildly acidic; avoid contact with eyes/skin.
• PPE: Laboratory coat, safety glasses, and appropriate chemical-resistant gloves. Handle powders in a fume hood or ventilated enclosure to minimize dust inhalation.
• Incompatibilities: Strong bases (may release TFA and promote peptide degradation), strong oxidants (thiol oxidation), and metal ions that catalyze oxidation of cysteinyl thiols. Use chelators (e.g., EDTA) if oxidation is a concern in solution work.
• First aid (overview, non-exhaustive): Rinse skin/eyes with water for 15 minutes; remove contaminated clothing. If inhaled, move to fresh air. If ingested, rinse mouth and seek medical attention. Always follow your institution’s SOPs.
• Special handling: Minimize exposure to air and moisture; peptides with free thiols are prone to disulfide formation. For anaerobic or reducing conditions, degas buffers and include reductants (e.g., DTT or TCEP) as appropriate for your application.

Research use only: Not for human or veterinary use.

Solvent Selection

Applicability: As a small, polar peptide salt, ACV Tripeptide TFA is handled predominantly in aqueous systems.

• Polarity/miscibility (literature/general)

  • Aqueous solubility: Generally high in water and aqueous buffers due to multiple ionizable groups and TFA counterion.
  • Organic solvents: Poorly soluble in nonpolar media (e.g., hexanes, toluene). Limited solubility in alcohols; mixtures with water (e.g., 50:50 MeOH/H2O) can aid handling.
  • pH effects: Solubility is typically greatest near acidic to neutral pH. Strongly basic media can promote degradation (β-elimination at cysteine, racemization) and counterion loss.

• Practical dissolving tips

  • Use ultrapure water or degassed buffers; gentle warming (room temp) and vortexing/sonication assist dissolution.
  • To preserve reduced cysteine, prepare solutions immediately before use and include reducing agents if compatible with your assay.

• Comparison (general)

  • TFA vs acetate salts: TFA salts dissolve readily but introduce non-volatile anions; acetate salts are more benign for some bioassays. If downstream lyophilization is needed, consider exchanging to volatile counterions (formate/acetate) after dissolution.

• When to choose alternatives

  • For hydrophobic derivatives or protected variants, 10–30% acetonitrile/water with 0.1% acid (formic/acetic) can improve solubility for analytical injections (HPLC/LC–MS).

Storage & Reconstitution

Item-specific storage/shipping

• Storage Conditions: Desiccated, Store at -80°C (from Product Data).
• Shipped In: Dry ice packs + Cold packs (from Product Data).

Item-specific reconstitution: Not specified for this item; refer to CoA/Spec Sheet.

General guidance (informational only)

• Allow container to equilibrate to room temperature in a desiccator before opening to avoid moisture condensation.
• Reconstitute in ultrapure water or appropriate buffer to a convenient concentration; filter if needed (0.22 μm) for sterile applications.
• Aliquot and refreeze at -80°C; avoid repeated freeze–thaw cycles. Consider adding reducing agents to maintain a free thiol state if compatible with downstream use.

Research use only: Not for human or veterinary use.

Structure & Identity

Brief overview: “ACV Tripeptide TFA” commonly refers (literature) to the trifluoroacetate salt of the nonribosomal tripeptide δ-(L-α-aminoadipyl)-L-cysteinyl-D-valine, the committed precursor in β-lactam (penicillin/cephalosporin) biosynthesis. This listing does not include a fully specified structure.

• Item-specific identifiers (from Product Data)

  • SKU: A1455672
  • Product Name: ACV Tripeptide TFA
  • CAS: A1455672 (catalog placeholder)
  • InChIKey: Not specified for this item; refer to CoA/Spec Sheet.
  • SMILES: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular Formula: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular Weight: Not specified for this item; refer to CoA/Spec Sheet.

• Structural description (literature/general)

  • Composition: L-α-aminoadipic acid (side-chain carboxylate), L-cysteine (thiol), and D-valine, joined by two amide bonds to form a tripeptide; commonly isolated as a TFA salt (protonated basic sites balanced by CF3CO2–).
  • Functional groups: carboxylates/carboxylic acids, amide bonds, a free thiol (unless protected/oxidized), and aliphatic side chains; one D-stereocenter (Val) with the remaining two L.
  • 2D description: HOOC-(CH2)3-CH(NH2)-CO–L-Cys(SH)–CO–D-Val–COOH (counterion: CF3CO2–), where termini and ionization states depend on pH and TFA association.

• Notes

  • If your workflow requires exact connectivity or salt stoichiometry, consult the product CoA/Spec Sheet for the definitive structure and counterion content.

Synthetic Utility

Literature perspective: ACV tripeptide is a uniquely positioned building block for chemoenzymatic synthesis of β-lactam frameworks.

• Functional group leverage

  • Two amide linkages define the peptide backbone; a free cysteinyl thiol and carboxyl termini provide handles for derivatization or conjugation (e.g., isotopic labeling, reporter tagging for mechanistic studies).

• Transformations (literature/general)

  • Enzymatic cyclization by IPNS to isopenicillin N (formation of β-lactam and thiazolidine rings) under mild, aqueous conditions.
  • Oxidation state control of cysteine (thiol ↔ disulfide) impacts reactivity; reducing conditions favor native substrate behavior.

• Retrosynthetic/analytical value

  • Serves as a reference scaffold to validate ACVS product fidelity and to benchmark noncanonical amino acid incorporation in engineered NRPS systems.
  • Useful as an LC–MS standard to quantify intracellular or extracellular levels of pathway intermediates.

• Practical considerations

  • Accurate molarity demands correction for counterion content and moisture (use CoA values).
  • Maintain low temperatures and exclude air/metal contaminants during handling to minimize degradation.

Target Specificity

Not applicable. This product is a small-molecule peptide substrate/standard, not an antibody, probe, or biological that exhibits defined species/epitope binding. No target specificity data are provided for this item.