Apidaecin IA , CAS No.123081-48-1

CAS: 123081-48-1 Cat. No.: A1416000 Formula: C₉₅H₁₅₀N₃₂O₂₃ Peso molecolare: 2108.41

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Panoramica

Apidaecin IA is an antibacterial peptide that can be found in honeybees.

Specifications

Condizioni di conservazione di stoccaggio

Store at -20°C

Spedito in

Ice chest + Ice pads

Questo prodotto richiede spedizione a catena fredda. I servizi di terra e altri servizi economici non sono disponibili.

Tipo di azione

INHIBITOR

Nomi e identificatori

• Peso molecolare: 2108.41

Application Protocols

No manufacturer-validated protocols are provided in the Product Data. The following are general, literature-style guidelines for research use only.

• Preparation of stock solutions (general)

• Warm vial to room temperature in a desiccator. Add sterile water or buffer to achieve 1–5 mg/mL. If needed, first wet with a small volume of 0.1% acetic acid, then dilute with buffer. Vortex gently and allow 5–10 min to dissolve. Filter sterilize (0.22 μm) if required.

• MIC assay (broth microdilution; general)

• Medium: Cation-adjusted Mueller–Hinton broth. Prepare two-fold serial dilutions of peptide across 96-well plate (e.g., 64 to 0.125 μg/mL). Inoculate with ~5×10^5 CFU/mL. Incubate 16–20 h at 35°C. Determine MIC as the lowest concentration with no visible growth/OD600 increase.

• Binding/biophysical assay setup (general)

• For fluorescence assays utilizing Tyr: Measure at λex ≈ 275 nm, λem ≈ 303 nm; adjust for inner-filter effects. For labeled analogs, follow fluorophore-specific settings and protect from light.

Adjust conditions to institutional SOPs and consult primary literature for organism- or target-specific parameters.

Biological Roles

• Origin and role (literature/general)

• Apidaecin IA is described as a proline-rich antimicrobial peptide (PR-AMP) from the innate immune system of the honeybee (Apis mellifera). It contributes to humoral defense against microbial invasion.

• Mechanistic themes (literature/general)

• Non-lytic antibacterial action predominantly against Gram-negative bacteria has been reported. Rather than disrupting membranes, PR-AMPs like Apidaecin interact with intracellular targets linked to protein synthesis (e.g., ribosome-associated factors). Specific target details may vary across studies and experimental systems.

• Biochemical properties (literature/general)

• Cationic nature promotes interaction with bacterial envelopes and facilitates uptake via inner-membrane transporters in some species.
• High proline content imparts a relatively rigid/extended conformation that can favor specific protein–protein interactions.

• Research significance

• Serves as a model system to understand AMP selectivity, bacterial uptake pathways, and resistance mechanisms. Extensively used for SAR to design stable, potent synthetic PR-AMP analogs.

Note: The above summarizes literature findings for context and does not imply any medical or clinical use. This product is for research use only.

Buffer Applications

This product is a research peptide and is not a buffering agent. It is not typically used to establish or maintain pH in biochemical experiments. For practical handling, see Storage & Reconstitution for dissolution guidance, and Solvent Selection for advice on aqueous media suitable for preparing peptide stocks.

Green Alternatives

• Context

• As a water-soluble peptide, Apidaecin-class materials are typically handled in aqueous media, aligning with green chemistry principles by reducing reliance on volatile organic solvents.

• Comparison (general; not item-specific)

• Aqueous buffers vs. organic solvents
  • Benefits: Minimal VOC emissions, improved safety, simplified waste handling.
  • Trade-offs: Potential microbial contamination of aqueous stocks; mitigate by sterile filtration and cold storage.
• Solid-phase peptide synthesis (SPPS) considerations (if preparing analogs in-house)
  • Greener alternatives to DMF/NMP (e.g., TamiSolve NxG, Cyrene) have been explored in literature, but process optimization is required to match coupling efficiency.

• Practical guidance

• Favor water or buffered saline for dissolution and assays.
• Use minimal percentages of organic modifiers (acetonitrile/methanol) only when required for solubility or chromatography.
• Manage peptide waste streams by segregating aqueous and organic fractions to facilitate appropriate disposal.

Pharmaceutical Uses

This material is offered for research use only. It is not an approved pharmaceutical ingredient and is not intended for human or veterinary use.

Within a laboratory/formulation research context (general):

• It may be used as a reference standard or tool compound in pre-formulation studies that investigate peptide stability, solubility, adsorption to containers, and excipient compatibility.
• Typical excipient roles (e.g., binder, disintegrant, tonicity agent) do not apply to this peptide. If used in prototype dosage forms for research, ensure all components and handling adhere to institutional and regulatory guidelines.

No pharmacopeial monograph, compendial status, or GMP grade is specified for this item; refer to the CoA/Spec Sheet for any item-specific quality declarations.

Physical Properties

• Item-specific data

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight (exact): Not specified for this item; refer to CoA/Spec Sheet.
• Water content, residual solvents, counter-ions/salt form: Not specified for this item; refer to CoA/Spec Sheet.

• Literature/general values and behavior (for context; not item specifications)

• Typical peptide state: Solid (often supplied lyophilized); highly hygroscopic depending on sequence.
• Approximate formula/MW (literature for Apidaecin 1a, sequence GNNRPVYIPQPRPPHPRL): MW ~2.1 kDa (monoisotopic ~2107–2109 Da depending on terminal state/salt). Use CoA for item-specific value.
• Solubility: Generally soluble in water and aqueous buffers; modest organic co-solvents (e.g., 10–20% acetonitrile) can aid dissolution if needed. Acidified water (0.1% acetic acid) can improve solubility/charge state for basic peptides. Avoid strong bases that can promote deamidation.
• pI/charge: Cationic at neutral pH due to Arg residues; His contributes pH-dependent charge (literature).
• LogP: Not applicable in the classical sense for peptides; strongly polar.
• Refractive index, density, BP/MP: Not meaningful for lyophilized peptides; thermal denaturation/decomposition occurs before melting/boiling.

• Practical notes (general)

• Reconstitute with high-purity water or buffer; filter sterilize if required for cell-based assays using low-protein-binding membranes (0.22 μm PTFE/PES).

Quality and Grades

• Item-specific quality information

• Grade/purity: Not specified for this item; refer to CoA/Spec Sheet.
• Counter-ion/salt form, sequence confirmation, residual solvents, and TFA content: Not specified for this item; refer to CoA/Spec Sheet.

• How to interpret common peptide quality metrics (general guidance)

• Purity (% area by HPLC): Reflects chromatographic homogeneity; ≥95% is common for research peptides intended for bioassays, while ≥98% may be preferred for SAR or analytical reference standards.
• Identity confirmation: Typically established by high-resolution MS and, where applicable, peptide sequencing/fragmentation (MS/MS). Exact mass should match the calculated monoisotopic or average mass for the specified sequence and terminal groups.
• Counter-ions: TFA and acetate are common; counter-ions can influence mass and solubility. If counter-ion content matters for your application, consult the CoA.
• Water and residual solvent: Karl Fischer and GC methods are used; moisture can impact accurate weighing of hygroscopic peptides.

• Stabilizers and additives

• Unless stated otherwise, research peptides are generally supplied neat (lyophilized) without carrier proteins. If stabilizers are present, they will be listed on the CoA and may affect downstream assays.

Reaction and Applications

• Manufacturer applications

• Not specified in the catalog entry; refer to the product page/CoA for any validated uses.

• Research applications (literature/general; for context only)

• Antimicrobial peptide studies: Benchmark PR-AMP used to probe non-lytic antibacterial mechanisms against Gram-negative bacteria.
• Mode-of-action research: Reported to interact with bacterial protein synthesis machinery and/or cytosolic chaperones (e.g., DnaK) in literature. Utilized to dissect ribosome-associated inhibition pathways without membrane disruption.
• Structure–activity relationship (SAR): Sequence variants and residue substitutions (e.g., Pro/Arg content, N-terminal modifications) are tested to tune potency, stability, and cell uptake.
• Biophysical assays: Employed in binding studies (ITC, MST), fluorescence assays (via Tyr intrinsic fluorescence or labeled analogs), and SPR to quantify interactions with bacterial proteins or model membranes.
• Microbiology workflows: Used in MIC determinations, time-kill kinetics, post-antibiotic effect, and resistance-development studies as a positive control PR-AMP.

• Practical tips (general)

• Prepare fresh aqueous stocks, minimize adsorption by using low-binding tips/tubes, and quantify concentration by weight or UV (Tyr ε280 ≈ 1490 M−1 cm−1, literature; adjust for sequence and counter-ions).

Reaction Conditions

This product is a peptide standard/tool compound rather than a small-molecule reagent used as a solvent or catalyst. Reaction-condition guidance below is provided as general literature context for modification or assay setup and is not item-specific.

• Chemical modification (general)

• NHS ester labeling (e.g., fluorescent dyes): pH 7.5–8.3 in phosphate or bicarbonate buffer; 1–2 h at room temperature; use 5–10× molar excess of reagent; protect from light; quench with Tris/glycine.
• Click chemistry (if azide/alkyne handles present via sequence engineering): CuAAC with CuSO4/sodium ascorbate/ligand in PBS or tert-butanol/water (1:1), room temperature to 37°C, 0.5–2 h; thoroughly remove copper post-reaction.

• Bioassay setup (literature/general)

• MIC testing against Gram-negative strains: Cation-adjusted Mueller–Hinton broth, inoculum ~5×10^5 CFU/mL, two-fold serial dilutions of peptide, 16–20 h incubation at 35±2°C; read OD600 or visual turbidity. Include sterility and growth controls.
• Time-kill assays: Fixed multiples of MIC, sampling over 0–24 h with CFU plating.

• Expected outcomes

• Labeling reactions typically reach >60–90% conversion under the above conditions depending on accessibility of reactive sites.
• MIC values vary by strain and conditions; consult primary literature for specific datasets on Apidaecin IA.

Safety and Handling

• GHS/SDS

• GHS classification, signal word, pictograms, H-statements: Not specified for this item; refer to SDS.

• General laboratory precautions (peptides; not a substitute for SDS)

• PPE: Laboratory coat, safety glasses, and appropriate gloves (nitrile). Use a dust mask or work in a fume hood/containment when handling powders to avoid inhalation.
• Avoid aerosol generation when weighing lyophilized material. Allow vial to equilibrate to room temperature in a desiccator before opening to minimize moisture uptake.
• Hygiene: Wash hands thoroughly after handling; avoid contact with skin, eyes, and clothing.

• Incompatibilities and stability (general)

• Avoid prolonged exposure to elevated temperature, moisture, and light. Peptides can undergo hydrolysis, deamidation (Asn), and oxidation (Tyr/His) under harsh conditions.
• Store as directed; keep tightly sealed with desiccant. For solutions, use low-binding plastics or silanized glass to reduce adsorption.

• First-aid overview (general)

• Inhalation: Move to fresh air; seek medical attention if symptoms persist.
• Skin/eye contact: Rinse with water for several minutes; remove contaminated clothing; seek medical advice if irritation persists.
• Ingestion: Rinse mouth; do not induce vomiting; obtain medical advice.

Always consult the product’s SDS for authoritative hazard information and local regulatory guidance.

Solvent Selection

• Polarity and miscibility (general for cationic peptides)

• Highly polar; readily soluble in water and most aqueous buffers. Limited solubility in nonpolar organic solvents. Small fractions of organic modifiers (acetonitrile, methanol) can assist dissolution.

• Practical solvent choices (general)

• Primary: Water (Type 1), PBS, or low-ionic-strength buffers at pH 5.0–7.4.
• To enhance initial dissolution: Add a minimal volume of 0.1% acetic acid or dilute HCl (e.g., 10 mM) to protonate basic residues, then bring to final volume with buffer.
• For stock solutions requiring sterility: Filter through 0.22 μm low-protein-binding membranes (PES/PTFE) and aliquot.
• Avoid high pH (>8.5) that can promote deamidation (Asn) or backbone cleavage over time.

• Comparison with alternatives (general)

• DMSO: Useful as a co-solvent for hydrophobic peptides; for Apidaecin-class peptides, typically not required but may be used up to 10–20% v/v if buffer capacity allows.
• Denaturants (e.g., 6 M guanidine HCl, 8 M urea): Can dissolve problematic aggregates but may interfere with bioassays; dialysis/desalting may be needed prior to biological testing.

• When to choose alternative media

• If adsorption losses are observed at low concentrations, include 0.05–0.1% carrier protein (e.g., BSA) in assay buffers or use siliconized glassware (general practice).

Storage and Reconstitution

• Item-specific storage

• Store at -20°C.
• Shipped in: Ice chest + Ice pads.

• General storage guidance for peptides (not item-specific)

• Lyophilized: Store desiccated, tightly capped, protected from light at -20°C or below. Under these conditions, many peptides remain stable for 12–24 months; confirm with CoA for this item.
• In solution: Prepare single-use aliquots to avoid repeated freeze–thaw. Store at -20°C for weeks to a few months or at 4°C for short-term (days). Avoid adsorption by using low-binding tubes and including carrier protein if working at low μg/mL levels.

• Reconstitution (general)

• Dissolve in high-purity water or compatible buffer to 1–5 mg/mL. If solubility is limited, pre-wet with 0.1% acetic acid, then dilute. Gently vortex; avoid vigorous foaming. Verify concentration gravimetrically or by UV if applicable (account for Tyr content and counter-ions).

• Stability notes (general)

• Minimize exposure to elevated pH, heat, and light. For long-term storage of solutions, consider sterile filtration and addition of antimicrobial agents only if compatible with downstream assays.

For any item-specific stability, purity, or sequence information, refer to the CoA/Spec Sheet.

Structure and Identity

• Item-specific identifiers

• Product name: Apidaecin IA (also styled Apidaecin 1a in literature)
• CAS: 123081-48-1
• Molecular formula: Not specified for this item; refer to CoA/Spec Sheet.
• Molecular weight: Not specified for this item; refer to CoA/Spec Sheet.
• SMILES: Not specified for this item; refer to CoA/Spec Sheet.
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet.

• Structural features (literature/general)

• Class: Proline-rich antimicrobial peptide (PR-AMP) isolated from honeybee hemolymph (Apis mellifera).
• Typical sequence reported for Apidaecin 1a: GNNRPVYIPQPRPPHPRL (18 residues). Variants exist; consult CoA for exact sequence if provided.
• Functional groups: Multiple primary amines (N-terminus, Arg side chains), imidazole (His), phenolic ring (Tyr), numerous secondary amides along the peptide backbone, high proline content imparting a relatively extended, polyproline-type conformation in water.
• Stereochemistry: Proteinogenic L-amino acids (literature), unless otherwise specified on the CoA.

• 2D/primary structure description (literature/general)

• Linear, cationic peptide with an N-terminus beginning in glycine/asparagine-rich segment, a central tyrosine and isoleucine conferring modest hydrophobic character, and a C-terminal region enriched in proline and arginine that drives binding to bacterial targets. No disulfide bonds are present in the canonical Apidaecin 1a sequence.

Synthetic Utility

• As a synthetic target (general)

• Linear, cationic peptide amenable to Fmoc/tBu solid-phase peptide synthesis (SPPS). High proline content generally facilitates coupling; attention to difficult residues (e.g., Arg(Pbf)) and prevention of diketopiperazine formation at early steps may be required.

• As a scaffold for derivatization (general)

• N-terminal modifications: Acetylation, fluorescent tags (e.g., FITC via diamino linkers), biotinylation, or isotopic labels for quantification.
• Side-chain conjugation: Exploit Lys/Arg scarcity by site-specific incorporation of orthogonally protected Lys or noncanonical amino acids (e.g., azidohomoalanine, propargylglycine) for click chemistry.
• C-terminal options: Amide vs. acid impacts net charge and stability; literature analogs often use C-terminal amide to mimic native processing.

• Retrosynthetic value

• Serves as a reference in designing shorter PR-AMP mimetics, peptidomimetics (e.g., β-peptides, peptoids), and chimeras that preserve antimicrobial activity while enhancing proteolytic stability and pharmacokinetics (research context).

• Analytical characterization (general)

• Confirm identity by HRMS and purity by RP-HPLC (C18, water/acetonitrile + 0.1% formic acid or TFA). Monitor potential Tyr oxidation (to DOPA/dimers) and Asn deamidation during storage/handling.

Target Specificity

Not applicable. This listing is not an antibody or affinity reagent, and no target-binding specificity, clone, isotype, or species reactivity data are provided in the Product Data. For general biological context on Apidaecin-class peptides, see the Biological Roles section.