C34 peptide , CAS No.C1421195

CAS: C1421195 Cat. No.: C1421195 Formula: C₁₈₆H₂₈₃N₅₁O₆₄S Peso molecolare: 4289.61

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Panoramica

C34 peptide is a biological active peptide. (This C34 peptide, also known as HR2, belongs to the helical region of gp41 of HIV , C-terminal heptad repeat 2 (HR2) defined as C helix or C peptide. It is known that HIV-1 enters cells by membrane fusion, C34 gp41 peptide is a potent inhibitors of HIV-1 fusion.)

Specifications

Condizioni di conservazione di stoccaggio

Store at -20°C

Spedito in

Ice chest + Ice pads

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Tipo di azione

INHIBITOR

Nomi e identificatori

• Peso molecolare: 4289.61

Application Protocols

No tested application protocols or performance parameters are provided for this item. The following are general planning notes to help design experiments; adjust to your system and consult the literature.

• Stock preparation (general)
  • Determine solvent strategy (water, buffer, or DMSO pre-dissolution) based on small-scale solubility tests. Filter (0.22 µm) if assay requires sterility.
• Working solutions
  • Prepare fresh before use. For assays sensitive to organic solvents, target ≤1–2% DMSO in final mixtures.
• Concentration determination
  • Use A280 if aromatic residues are present; otherwise, rely on peptide content and mass from the CoA or perform amino acid analysis.
• Controls
  • Include vehicle-only controls and, if available, sequence-scrambled or truncated peptide controls for specificity assessment.
• Storage during studies
  • Keep on ice during prolonged handling; avoid repeated freeze–thaw by aliquoting stocks.

For any application-specific parameters (e.g., concentrations, incubation times, detection modalities), consult primary literature for the exact C34 sequence of interest and adapt conditions accordingly. Item-specific protocols are not specified for this SKU.

Biological Roles

No item-specific biological annotations are provided. The following describes literature/general roles associated with “C34”-designated peptides without making therapeutic claims.

• Context (literature/general)
  • C34 typically denotes a 34-residue segment derived from a class I viral fusion protein heptad-repeat region used to interrogate membrane fusion mechanisms in vitro.
  • Such peptides can form α-helical structures and engage complementary heptad-repeat targets, serving as tools to study six-helix bundle formation and fusion activation steps in model systems.
• Research uses enabled by these roles
  • Dissecting peptide–protein interactions involved in membrane apposition and lipid mixing using liposome or supported bilayer assays.
  • Benchmarking biophysical parameters (helicity, thermal stability, binding affinity) in response to sequence modifications (e.g., salt bridges, helix-stabilizing substitutions) to map structure–function relationships.
  • Serving as positive/negative controls in coiled-coil or fusion-peptide binding assays and for calibrating computational models of helix–helix packing.
• Considerations for experimental design (general)
  • Amphipathic helices can self-associate; ionic strength, pH, and the presence of mild detergents or membrane mimetics strongly affect observed behavior.
  • Specificity is sequence-determined; verify the exact sequence and any terminal modifications from the CoA/Spec Sheet before interpreting results.
  • For quantitative comparisons across studies, report counterion, peptide content (%), buffer composition, temperature, and pre-treatment (e.g., annealing/heating–cooling cycles).

Buffer Applications

No item-specific buffer recommendations are provided. The following are general, literature-based practices for dissolving and handling research peptides.

• Initial dissolution strategy (general)
  • Hydrophilic/basic peptides: Dissolve in water or 0.1% acetic acid or 0.1% TFA; adjust to working buffer after full dissolution.
  • Acidic peptides: Dissolve in 10–50 mM Tris or HEPES at pH 8.0–8.5; alternatively, 50–100 mM ammonium bicarbonate (volatile) for MS workflows.
  • Hydrophobic peptides: Wet with a minimal volume of DMSO or isopropanol, then titrate in buffer (e.g., PBS, HEPES) with mixing to reach the desired concentration.
• Common buffer systems (literature/general)
  • Phosphate buffer (PBS or 10–50 mM sodium phosphate): pH 6.5–7.5; good for CD and fluorescence if ionic strength is controlled.
  • HEPES (10–50 mM): pH 7.0–8.0; low UV absorbance above 230 nm, suitable for optical assays.
  • Acetate (10–50 mM): pH 4.5–5.5 for basic peptides; gentle on acid-labile residues.
• Practical tips
  • Gentle warming (25–37°C) and brief sonication can aid dissolution; avoid prolonged heating.
  • Filter through 0.22 µm if required; some peptides adsorb to filters—pre-rinse with buffer containing 0.01–0.1% carrier protein or 0.01% mild detergent if compatible with your assay.
  • For concentration determination, use A280 if aromatic residues are present; otherwise, determine by peptide content from CoA or amino acid analysis.

Green Alternatives

Peptide handling is largely aqueous, enabling inherently greener practices. Where organic co-solvents are needed, select minimal volumes and safer alternatives. Item-specific requirements are not provided; guidance below is general/literature-based.

• Prefer aqueous buffers

  • Use water, phosphate, HEPES, or acetate buffers whenever possible. Optimize pH/ionic strength to improve solubility and reduce reliance on organics.

• Solvent hierarchy (greener choices vs typical)

  Greener choice | Typical choice | Comments (general) ---------------|----------------|------------------- Water/buffer | DMSO | Start in water; if insoluble, prepare a DMSO concentrate and dilute promptly. Assess assay tolerance. Ethanol | Acetonitrile | Ethanol has lower toxicity; limited UV transparency vs ACN for some optical assays. Isopropanol | DMF | Useful for initial wetting; avoid high fractions in bioassays.

• Process considerations

  • Use small-volume, high-concentration stocks to reduce solvent use and waste.
  • Avoid halogenated solvents; rarely necessary for peptide dissolution.
  • Choose low-energy storage (-20°C) with desiccation rather than repeated lyophilization cycles.

• Waste minimization

  • Consolidate dilute aqueous peptide wastes; avoid adding unnecessary denaturants or dyes unless required.
  • Validate solubility at micro-scale to prevent large failed preparations.

• Trade-offs

  • DMSO remains the most reliable solvent for highly hydrophobic peptides; its use may be unavoidable. Balance with lower final percentages and prompt dilution into aqueous media.

Pharmaceutical Uses

No pharmacopeial or excipient status is provided for this item, and it is sold strictly for research use only.

• Research-use-only notice
  • The Product Data specify: For research use only. Not for human or veterinary use, diagnostic procedures, or clinical applications.
• Formulation and manufacturing context (general/literature)
  • In research settings, peptides like C34 are formulated as aqueous stocks or lyophilized aliquots for in vitro assays and biophysical studies.
  • Typical excipients used in research formulations include mannitol, trehalose, or glycine as bulking stabilizers for lyophilization; these are not specified for this item.
  • Buffer selection emphasizes stability of secondary structure and prevention of aggregation; ionic strength and pH are tuned empirically.
• Regulatory/compendial status
  • No USP/EP monograph or excipient designation is implied by this listing. Any GMP/clinical use would require separate qualification and is outside the scope of this product.
• Practical note
  • If your laboratory requires specific endotoxin/bioburden, residual solvent, or counterion limits, request and review the CoA/Spec Sheet and, if necessary, an expanded QC package. Item-specific values are not specified for this SKU.

Physical Properties

Item-specific constants are not provided in the Product Data for this SKU. Consult the CoA/Spec Sheet for definitive values.

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Melting point / decomposition: Not specified for this item; refer to CoA/Spec Sheet. (Peptides typically do not exhibit a sharp melting point and often decompose on heating; literature/general.)
• Solubility (general/literature guidance)
  • Aqueous buffers: Sequence-dependent; many peptides dissolve in water, PBS, or low-ionic-strength buffers. Hydrophobic sequences may require initial dissolution in DMSO or dilute acetic acid, then aqueous dilution.
  • Organic co-solvents: DMSO is most common; small fractions of acetonitrile or ethanol can assist solubilization (literature).
  • pH dependence: Basic peptides often dissolve better in mildly acidic solutions (e.g., 0.1% TFA or acetic acid); acidic peptides may require mildly basic buffers (e.g., 10–50 mM Tris, pH 8) (literature).
• pKa/logP: Not applicable as single values; properties are sequence-dependent (literature).
• Hygroscopicity: Lyophilized peptides can be hygroscopic and absorb moisture/CO2; handle under dry conditions (general).
• Optical properties: Aromatic residues (Trp/Tyr/Phe) contribute to UV absorbance (280 nm for Trp/Tyr) for concentration estimation; extinction coefficient is sequence-dependent (literature).
• Refractive index/density: Not typically reported for peptides; Not specified for this item.

Quality and Grades

Item-specific grade and purity are not provided in the Product Data. Refer to the CoA/Spec Sheet for definitive quality metrics for C34 peptide.

• What peptide grade typically implies (general/literature)
  • Crude: Minimal post-synthesis cleanup; contains deletion sequences, protecting-group remnants, and side products.
  • Desalted: Low-molecular-weight impurities removed; sequence-related impurities may remain.
  • Purified (e.g., >90%, >95%, >98% by HPLC): Enriched for the target sequence; residual closely related impurities may persist.
  • MS-validated: Confirms molecular mass of principal component (e.g., ESI/ MALDI) within method tolerance.
  • Counterion form: Frequently isolated as TFA salt; alternative counterions (acetate, HCl) may be specified. Counterion impacts mass, solubility, and bioassay background.
• Typical QC documentation (general)
  • Analytical RP-HPLC chromatogram (with gradient, wavelength, and retention time).
  • Mass spectrometry data (observed vs calculated m/z for principal charge states).
  • If applicable: Amino acid analysis, peptide content %, water/ash content, residual solvents, endotoxin/bioburden for specialized research needs.
• Guidance specific to this item
  • Grade/purity: Not specified for this item; refer to CoA/Spec Sheet.
  • Additives/stabilizers and salt form: Not specified for this item; refer to CoA/Spec Sheet.
  • Sequence and modifications (e.g., acetylation/amidation): Not specified for this item; confirm on CoA before method development.

Reaction and Applications

This peptide is intended for research use. While peptides are not “reagents” in the classical synthetic sense, C34-designated peptides are commonly employed as functional biomolecules in mechanistic and biophysical studies. Item-specific application testing is not provided; the following reflects general/literature practice.

• Biophysical/biochemical applications (literature/general)
  • Protein–peptide interaction studies by SPR, BLI, ITC, MST, or fluorescence anisotropy to quantify binding to cognate heptad-repeat coiled-coil targets.
  • Structural characterization: Circular dichroism (CD) for helicity/thermal stability; NMR for residue-level interactions in membrane-mimetic environments (e.g., DPC micelles, bicelles).
  • Membrane/fusion model systems: Liposome leakage or fusion assays using fluorescent probes to interrogate peptide effects on lipid mixing (research models).
• Assay development tips
  • Use freshly prepared stocks; many amphipathic peptides self-associate in aqueous media—include salt (100–150 mM NaCl) or gentle detergents (e.g., 0.01% DDM) as appropriate.
  • For hydrophobic sequences, pre-dissolve in DMSO, then dilute into assay buffer under vigorous mixing to prevent precipitation. Keep final DMSO ≤1–2% if assay-sensitive.
  • Determine concentration by UV at 280 nm if Trp/Tyr present; otherwise use quantitative amino acid analysis or gravimetry with peptide content correction from CoA.
• Chemical derivatization (general)
  • N-terminal/C-terminal conjugation (NHS ester dyes, sulfo-NHS biotin), thiol-specific labeling if Cys is present (maleimide, iodoacetamide), and click chemistry handles if orthogonal azido/alkynyl residues were incorporated (sequence-dependent; not specified for this item).

Reaction Conditions

No item-specific reactive functional groups are provided. The following general, literature-based conditions apply to common peptide conjugation chemistries; adapt to your sequence and assay.

• Amine labeling (N-terminus/Lys) with NHS esters (general)
  • Buffer: 50–100 mM phosphate or bicarbonate, pH 7.5–8.5; avoid primary amine buffers (e.g., Tris) during coupling.
  • Solvent: Aqueous with ≤10–20% DMSO or DMF to solubilize hydrophobic dyes.
  • Temperature/time: Room temperature for 30–120 min; monitor by LC–MS.
• Thiol labeling at Cys (maleimide) (general)
  • Buffer: 50 mM phosphate/HEPES, pH 6.5–7.5; include 1–5 mM EDTA; avoid competing thiols (e.g., DTT) during conjugation.
  • Temperature/time: 0–25°C, 15–60 min; quench unreacted maleimide with cysteine or mercaptoethanol.
• Disulfide formation/exchange (general)
  • Oxidation: Air or mild oxidants (e.g., 0.1% DMSO) at pH 7–8; monitor to avoid overoxidation.
• Click chemistry (CuAAC; if azide/alkyne present) (general)
  • Buffer: Aqueous with t-BuOH or DMSO co-solvent; pH 7–8.
  • Catalyst: CuSO4 with ligand (e.g., TBTA) and sodium ascorbate; degas to limit side reactions.
• Purification/analysis
  • Desalt or purify by RP-HPLC (C18) with water/acetonitrile + 0.05–0.1% TFA or formic acid; verify by MS and analytical HPLC.
• Yields and kinetics
  • Highly sequence- and reagent-dependent; optimize stoichiometry (typically 1.2–5 eq label per reactive site) and confirm by analytical methods.

Safety and Handling

Authoritative safety information resides in the product SDS. Item-specific GHS details are not provided in the Product Data.

• GHS/Classification (item-specific)
  • Signal word: Not specified for this item; refer to SDS.
  • Hazard statements (H-codes): Not specified for this item; refer to SDS.
  • Pictograms: Not specified for this item; refer to SDS.
• General laboratory safety for peptides (literature/general)
  • Expected hazard profile: Synthetic peptides are generally of low volatility and low acute toxicity via inhalation; avoid inhalation of powders and contact with skin/eyes.
  • PPE: Lab coat, safety glasses, and appropriate gloves (nitrile). Use a dust mask or work in a fume hood/ventilated enclosure when handling powders.
  • Handling: Minimize exposure to atmospheric moisture; allow vial to equilibrate to room temperature in a desiccator before opening to prevent condensation.
  • First aid (overview): If inhaled, move to fresh air; if on skin/eyes, rinse with water for several minutes; if ingested, rinse mouth. Seek medical advice and present SDS.
• Incompatibilities (general)
  • Strong oxidizers can modify susceptible residues (Met, Cys, Trp, Tyr). Avoid prolonged exposure to elevated pH (>9) or temperatures that may cause deamidation, racemization, or backbone hydrolysis.
  • Light/oxygen sensitivity: Peptides containing Trp, Met, Cys, or His may be light/air sensitive; protect from light and use inert atmosphere for long-term storage when feasible.
• Waste disposal: Dispose of aqueous solutions and solids according to institutional and local regulations for non-halogenated organic/biochemical waste; consult SDS.

Solvent Selection

Because peptides exhibit sequence-dependent solubility, solvent choice should be guided by small-scale tests. No item-specific solubility data are provided; the following are general, literature-based best practices.

• Primary solvents
  • Water or buffer (e.g., Milli-Q water, PBS, 10–50 mM HEPES/Tris): Use for hydrophilic/charged sequences.
  • Dilute acids/bases: 0.1–1% acetic acid or 0.1% TFA can improve solubility of basic peptides; 10–50 mM ammonium bicarbonate or Tris pH 8–8.5 can help acidic peptides (literature).
  • DMSO: Effective for hydrophobic peptides; prepare a concentrated stock (e.g., 10–50 mM), then dilute into aqueous media with vigorous mixing to avoid precipitation (general practice).
• Co-solvent strategies
  • 5–20% acetonitrile or ethanol in buffer can assist dissolution while maintaining compatibility with many bioassays (verify assay tolerance).
  • Additive salts (100–200 mM NaCl) may reduce aggregation for some amphipathic helices.
• Decision cues (general)
  • If the peptide contains many basic residues (Arg/Lys): try mildly acidic aqueous media first.
  • If enriched in acidic residues (Asp/Glu): try mildly basic buffers.
  • If aromatic/hydrophobic: begin with DMSO or isopropanol micro-volume wetting, then stepwise aqueous dilution.
• Compatibility notes
  • Avoid high concentrations of organic cosolvents in cell-free enzyme assays sensitive to solvent.
  • For spectroscopic work (CD, fluorescence), prefer low-absorbance buffers (e.g., phosphate or HEPES) and minimize organic content.
• Final check: Filter (0.22 µm) if needed; confirm clarity and stability over the experimental time frame.

Storage and Reconstitution

The Product Data specify: Store at -20°C. Shipped in an ice chest with ice pads. Additional handling guidance below is general best practice for research peptides.

• Upon receipt
  • Inspect the container for integrity. Allow the unopened vial to equilibrate to room temperature in a desiccator before opening to avoid condensation.
• Storage (item-specific + general)
  • Long-term: -20°C in a dry, dark environment. For extended storage, -80°C can further mitigate degradation (general). Protect from moisture and light.
  • Lyophilized state: Typically most stable when kept dry with desiccant and inert headspace (general).
  • In solution: Store aliquots at -20°C or lower; avoid repeated freeze–thaw cycles. Stability in solution is sequence- and buffer-dependent; prepare fresh as needed.
• Reconstitution (general)
  • Select solvent based on sequence: water/buffer for hydrophilic peptides; 0.1% acetic acid or TFA for basic peptides; DMSO pre-dissolution for hydrophobic sequences.
  • Gently vortex and, if necessary, briefly sonicate. Mild warming (25–37°C) can help. Do not overheat.
  • Filter sterilize (0.22 µm) if sterility is required. Note potential adsorption to filters; pre-wet with buffer containing compatible carrier if needed.
• Aliquoting and record-keeping
  • Prepare single-use aliquots to prevent freeze–thaw. Label with concentration, solvent, counterion (if known), and date.
• Specifications
  • Appearance, purity, counterion, and exact sequence: Not specified for this item; refer to CoA/Spec Sheet.
  • Research Use: For research use only.

Structure and Identity

Brief description: C34 peptide is a synthetic research peptide. Specific identifying constants for this catalog item are not provided in the Product Data; consult the CoA/Spec Sheet for definitive identity metrics.

• Item-specific identifiers
  • Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
  • Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
  • CAS: C1421195 (catalog placeholder)
  • InChIKey: Not specified for this item; refer to CoA/Spec Sheet.
  • SMILES: Not applicable/typically undefined for polypeptides; Not specified for this item; refer to CoA/Spec Sheet.
• Structural class and features (general/literature)
  • Type: Synthetic polypeptide (linear) composed of α-amino acids linked by peptide (amide) bonds.
  • Functional groups: Multiple amide linkages along the backbone; side-chain functionalities depend on sequence (e.g., carboxylates, amines, alcohols, thioethers, aromatics) (literature/general).
  • End-group chemistry: Peptides may be supplied with free/blocked termini (e.g., free N-terminus, acetylation; free C-terminus, amidation) depending on synthesis (not specified for this item).
• 2D structure description (general)
  • Backbone: Repeating –NH–CH(R)–CO– units forming a linear chain; side chains R project alternately from the plane of the backbone.
  • Stereochemistry: Proteinogenic residues typically L-configuration at Cα unless otherwise stated (not specified for this item).
• Naming context (literature/general)
  • The designation “C34” commonly refers to a 34-residue peptide segment used to study class I viral fusion mechanisms; exact sequence and modifications for this SKU are not specified and should be confirmed on the CoA/Spec Sheet.

Synthetic Utility

While peptides are not conventional small-molecule reagents, a C34-length peptide can serve as a versatile scaffold in chemical biology. The following reflects general/literature practices and does not assert specific features for this SKU.

• Functional handles (sequence-dependent; not specified for this item)
  • Free N-terminus (amine) or C-terminus (carboxylate or amide) for conjugation.
  • Side chains: Lys (ε-amine), Cys (thiol), Asp/Glu (carboxylates), Ser/Thr/Tyr (alcohol/phenol) as chemoselective points of attachment.
• Common transformations (general)
  • NHS ester coupling to N-terminus or Lys for fluorophores/biotin/PEG.
  • Thiol–maleimide or disulfide exchange for site-specific labeling at Cys.
  • Click chemistry (CuAAC/SPIEDAC) when azido/alkynyl or tetrazine/TCO handles are introduced via noncanonical residues.
  • Peptide stapling (e.g., all-hydrocarbon i,i+4) or lactam bridges to stabilize helicity (requires appropriate residues; not specified for this item).
• Retrosynthetic/assembly considerations
  • Solid-phase peptide synthesis (SPPS) using Fmoc/tBu chemistry with orthogonal protection enables sequence-specific placement of labels and post-synthetic modifications.
  • Counterion exchange (e.g., TFA→acetate) can be performed post-cleavage to improve downstream assay performance.
• Practical guidance
  • Plan site-specific conjugation to preserve functional binding interfaces; map surface-exposed residues via modeling or NMR/CD perturbations.
  • Validate integrity after modification by LC–MS and, if relevant, by analytical RP-HPLC and CD to confirm secondary structure retention.

Target Specificity

Item-specific target, epitope, or binding specificity data are not provided for this SKU.

• Target/epitope: Not specified for this item; refer to CoA/Spec Sheet.
• Species reactivity: Not specified for this item; refer to CoA/Spec Sheet.
• Clone/isotype: Not applicable.

Note: For peptides used as binders or inhibitors in research, specificity is determined by exact sequence and modifications. Verify sequence and intended binding partner from the CoA/Spec Sheet and relevant literature before designing experiments.