GPLGIAGQ TFA - ≥99% , CAS No.109053-09-0(free)

CAS: 109053-09-0(free) Cat. No.: G658993 Formula: C₃₁H₅₃N₉O₁₀(free) Peso molecolare: 711.8(free)

QUALITÀ & PUREZZA ≥99%

Storage

Store at -20°C,Desiccated

Shipped In

Ice chest + Ice pads

Panoramica

GPLGIAGQ TFA, a MMP2-cleavable polypeptide, is used as a stimulus-sensitive linker in both liposomal and micellar nanocarriers for MMP2-triggered tumor targeting. GPLGIAGQ TFA can be used to synthesis unique MMP2-targeted photosensitizer in photodynamic therapy (PDT).

Specifiche

Specifiche e purezza

≥99%

Condizioni di conservazione di stoccaggio

Store at -20°C,Desiccated

Spedito in

Ice chest + Ice pads

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

Purezza

≥99%

Nomi e identificatori

Peso molecolare

711.8(free)

Proprietà chimiche e fisiche

• Solubilità: DMSO : 50 mg/mL (60.55 mM; Need ultrasonic)
• Sensibilità: Moisture sensitive

Application Protocols

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

• Example literature protocol: Preparation of a stock solution

  • Bring vial to room temperature in a desiccator before opening to prevent condensation.
  • Dissolve peptide in sterile water or a minimal volume of DMSO (e.g., 10–20 mg/mL), then dilute with buffer to the desired working concentration. If needed, adjust pH to 7.2–7.5 (TFA salt solutions may be acidic).
  • Sterile-filter through a 0.22 µm membrane for cell-related assays.
  • Aliquot and store at −20°C to avoid repeated freeze–thaw cycles.

• Example literature workflow: Protease challenge and LC–MS verification (unlabeled core)

  • Incubate peptide (e.g., 20 µM) with the protease of interest in a suitable buffer at 37°C.
  • Quench at timepoints by acidification (e.g., 1% formic acid) and analyze by LC–MS to observe appearance of expected fragments around the Gly–Ile region (sequence-context dependent).
  • Include controls: no-enzyme, heat-inactivated enzyme, and EDTA-inhibited (for metalloproteinases) to assess specificity.

• Note: The above are general, literature-based examples and not validated for this specific lot. Optimize conditions for your system.

Biological Roles

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

• Literature/general (no therapeutic claims):

  • Recognition motif: The GPLGIAGQ sequence belongs to a family of Gly–Pro–Leu–Gly–Ile–Ala–Gly-containing motifs frequently used as recognition/cleavage sites for matrix metalloproteinases (MMPs), particularly gelatinases (MMP-2/MMP-9). Such motifs are inspired by sequences found in collagen/gelatin domains where MMPs natively act.
  • Biochemical behavior: As an unmodified peptide, it does not possess intrinsic receptor-mediated biological activity; instead, its utility arises from serving as a selective substrate segment for endopeptidases in vitro or in engineered constructs.
  • Stability considerations: Susceptible to proteolysis by target and off-target proteases; Gln can undergo slow deamidation under basic conditions; backbone hydrolysis accelerates at extremes of pH and temperature.
  • Use in assay design: Commonly embedded between reporter pairs (e.g., fluorophore–quencher) or between a carrier and a payload to monitor or induce cleavage under enzymatic challenge. Kinetic parameters (kcat/KM) depend strongly on sequence context, labeling, and assay buffer; consult primary literature when quantitative specificity is required.
  • Cellular context: When applied to cells, uptake and stability are low without modification; N-terminal acetylation/C-terminal amidation or PEGylation can improve stability for mechanistic studies (research use only).

Buffer Applications

This product is a peptide substrate/linker and is not itself a buffering reagent. It does not form a conventional biological or electrophoresis buffer system.

• Practical note: When preparing solutions, select a buffer compatible with your downstream application (e.g., HEPES, Tris, or phosphate at pH 7.0–7.5 for metalloproteinase assays). Include required cofactors (e.g., Ca2+, Zn2+ for MMP activity) and avoid chelators if enzymatic activity is desired.

• For HPLC handling, volatile acids (0.1% formic or acetic acid) can replace TFA when MS detection is planned, recognizing potential changes in retention and peak shape.

Green Alternatives

• Context: As a solid peptide, the primary “green” considerations are solvent choice for dissolution/purification and the counterion (TFA) burden.

• Greener choices (literature guidance):

  • Counterion exchange: Replace TFA with acetate or bicarbonate salts to reduce persistent fluorinated anions in waste streams. Simple protocols include repeated dissolution in aqueous ammonium bicarbonate followed by lyophilization.
  • Solvents for workup/purification: Favor water, ethanol (where compatible), and isopropanol over acetonitrile for non-critical steps. In HPLC, consider reducing TFA concentration or substituting with formic/acetic acid when MS sensitivity is required.
  • Solid-phase synthesis improvements (if preparing analogs): Use greener coupling reagents (e.g., COMU, OxymaPure with EDC) and minimize DMF/DCE by adopting greener solvents (N-butylpyrrolidone, propylene carbonate) where validated.

• Comparison (illustrative; literature):

  • TFA vs acetate counterion
    • Environmental: TFA is persistent; acetate is biodegradable.
    • Performance: TFA improves RP-HPLC peak shape via ion pairing; acetate is milder but may broaden peaks.
  • Acetonitrile vs ethanol/water for prep steps
    • ACN: Excellent peptide solvation, volatile but petrochemical.
    • EtOH/H2O: Safer and renewable; may require longer dissolution times or mild heating.

• Trade-offs: Greener buffers/acids can slightly change peptide retention and assay conditions; re-optimize gradients and pH to maintain performance.

Pharmaceutical Uses

No clinical/therapeutic claims are made. For research and development purposes only.

• Literature/general formulation roles:

  • Cleavable linker research: GPLGIAGQ-like motifs are studied as enzymatically cleavable spacers in bioconjugation (e.g., antibody–drug conjugates, polymer–drug conjugates) where protease-rich environments trigger release of payloads. Such studies require rigorous characterization of stability and cleavage kinetics.
  • Excipient status: Not a pharmacopeial excipient. When peptides are used in preformulation studies, typical vehicles include aqueous buffers with isotonic modifiers; however, this sequence is primarily a functional linker/substrate rather than an excipient.
  • Salt form: TFA salt is common from purification; for pharmaceutical development, counterion exchange (e.g., to acetate or HCl) is often performed to reduce residual TFA.
  • Analytics: Release testing in simulated fluids and protease panels, LC–MS monitoring of fragments, and peptide mapping are standard tools in formulation feasibility studies.

• Manufacturing considerations (research stage):

  • Control of residual solvents, counterions, and water content.
  • Specification of peptide purity and impurity profile (deletions/truncations) to ensure predictable cleavage behavior.

Physical Properties

• Item-specific (from Product Data):

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

• Literature/general expectations for small peptides (informational, not specifications):

  • Physical state: white to off-white solid (typical for lyophilized peptides).
  • Solubility guidance: Many short peptides are soluble in water, aqueous buffers, and polar aprotic solvents (e.g., DMSO). Hydrophobic residues (Leu, Ile) may reduce aqueous solubility; initial dissolution in a minimal volume of DMSO (or dilute aqueous base ~pH 8) followed by aqueous dilution is a common approach. The TFA counterion can acidify solutions; adjust pH if required for assays.
  • pH behavior: Free N-terminus (basic), C-terminus (acidic), and a neutral Gln side chain; overall ionization is sequence- and pH-dependent. Isoelectric behavior is dominated by the terminal groups (no Lys/Arg/Asp/Glu present).
  • Hygroscopicity: Peptides and TFA salts may be hygroscopic; handle quickly at ambient humidity to avoid moisture uptake.
  • Melting/boiling points, density, logP, refractive index: Not generally defined/used for peptides; not applicable for routine lab use.

• Practical notes (literature):

  • Filter sterilization typically uses 0.22 µm PVDF or PES after dissolution.
  • For accurate concentrations, determine peptide content by dry mass with correction for counterions/residual water if available on CoA, or use UV at 205 nm with an extinction coefficient method for peptides lacking aromatics.

Quality and Grades

• Item-specific (from Product Data):

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

• General notes on peptide quality (literature/context):

  • Typical peptide offerings are specified by purity determined via analytical RP-HPLC (e.g., >90%, >95%, or >98%) with identity confirmed by MS (ESI/MALDI) and sometimes by NMR for small sequences. In absence of a stated grade, verify lot-specific purity, form (acetate vs TFA salt), counterion content, and water/solvent content on the CoA.
  • TFA salt vs acetate/HCl: TFA provides strong ion-pairing and is commonly used in RP-HPLC purification. Residual TFA can influence bioassays and cell-based systems; where low TFA is required, consider counterion exchange to acetate or HCl post-purchase.
  • Content determination: Reported net peptide content (NPC) accounts for residual moisture, counterions, and salts. This is essential for accurate molar dosing; if NPC is not provided, consider Karl Fischer (water) and anion quantification or use amino acid analysis.
  • Impurity profile: Typical impurities include deletion sequences, truncations, and protecting group remnants. For protease substrate applications, confirm that critical positions (e.g., the P3–P1’ motif) are intact at high purity to avoid kinetic artifacts.
  • If you require specific specification thresholds (e.g., TFA ≤0.1%, peptide purity ≥95%), please request custom grade with detailed acceptance criteria.

Reaction and Applications

• Item-specific applications (from Product Data):

  • Manufacturer applications: Not specified for this item; refer to catalog/CoA.

• Literature/general applications relevant to GPLGIAGQ motif:

  • Metalloproteinase substrate motif: Sequences containing GP–LG–IAG are widely used as recognition/cleavage sites for matrix metalloproteinases (MMP-2/MMP-9 and related MMPs) in fluorogenic, chromogenic, and mass-spec–based protease assays. The scissile bond is typically reported around the Gly–Ile position in related motifs (literature), though exact kinetics depend on flanking residues and assay conditions.
  • Linker design: Used as a cleavable linker core in prodrug/bioconjugate and polymer–drug conjugate research, where MMP-rich microenvironments mediate release (e.g., GPLG↓IAGQ-derived motifs in ADC and hydrogel systems; literature).
  • Materials: Embedded in peptide–polymer hybrids to confer enzyme-responsiveness for controlled degradation.
  • Analytical tool: Serves as an unlabeled core sequence to be derivatized (e.g., fluorophore–quencher pairs at N- and C-termini) for building FRET substrates.

• Practical tips (literature):

  • For conjugation, protect N-terminus (e.g., acetylation) or C-terminus (e.g., amide) as needed to direct coupling. Incorporate spacers (Ahx/PEG) to reduce steric hindrance.
  • In protease assays, maintain Zn2+ and Ca2+ where required for MMP activity; avoid metal chelators (EDTA) unless performing inhibition controls.
  • Validate cleavage by LC–MS to confirm expected fragments and to rule out nonspecific hydrolysis.

Reaction Conditions

• General coupling/deprotection conditions for peptide modification (literature guidance):

  • Amide couplings: Use HATU or HBTU (3–5 equiv) with DIPEA (4–8 equiv) in DMF or NMP at 0.05–0.2 M, 0.5–2 h at rt; monitor by LC–MS. Greener alternatives include EDC·HCl (1.5–2.0 equiv) with OxymaPure (1.5–2.0 equiv) in NBP/EtOAc mixtures.
  • N-terminal acylation: NHS-esters (2–5 equiv) in buffered aqueous-organic mixtures (pH 7.5–8.5) for 0.5–2 h; keep organic cosolvent ≤30% to maintain peptide solubility and minimize hydrolysis of NHS.
  • C-terminal activation: Convert to active esters (e.g., pentafluorophenyl) or use carbodiimide coupling (EDC) with amines under mildly basic conditions (pH 7.5–8.0).
  • Click chemistry handles: Introduce azide (via N3–linker NHS) or alkyne (via propiolate NHS) at the N-terminus, then perform CuAAC (CuSO4/sodium ascorbate, tBuOH/H2O 1:1, rt, 1–3 h) or SPAAC (strain-promoted) for bioconjugation.

• Protease assay conditions (illustrative, literature-only):

  • Buffer: 50 mM Tris–HCl, 150 mM NaCl, 10 mM CaCl2, 0.05% Brij-35, pH 7.5; include Zn2+ as required by enzyme source.
  • Temperature: 25–37°C.
  • Substrate concentration: typically 1–50 µM; enzyme in the low nM range depending on activity.
  • Readout: For labeled analogs, monitor fluorescence increase (e.g., Ex/Em per dye); for unlabeled cores, track cleavage by LC–MS.

• Stability cautions:

  • Avoid >pH 9 for extended periods (backbone cleavage, deamidation of Gln). Minimize exposure to oxidants and elevated temperatures. Use freshly prepared solutions.

Safety and Handling

• Item-specific (from Product Data):

  • GHS classification: Not specified for this item; refer to SDS.
  • Signal word / H-statements / pictograms: Not specified for this item; refer to SDS.
  • Storage conditions: Store at −20°C, desiccated. Shipments are provided cold (ice chest + ice pads).
  • Research Use: For research use only.

• General safety guidance for peptides and TFA salts (literature; not a substitute for SDS):

  • Hazards: Unmodified research peptides are typically of low acute toxicity but may cause irritation to eyes, skin, and respiratory tract as fine powders. Residual TFA or TFA salt content can render solutions acidic.
  • PPE: Wear lab coat, safety glasses, and appropriate disposable gloves (e.g., nitrile). Avoid inhalation of dust and contact with skin/eyes.
  • Handling: Work in a clean, dry environment. Open vials at ambient temperature to avoid condensation, then promptly re-cap or desiccate. Use local exhaust/hood if dust generation is possible.
  • Incompatibilities: Strong oxidizers and strong bases/acids can degrade peptides; avoid prolonged exposure to high pH (>9) or low pH (<2) unless intended. Prevent repeated freeze–thaw cycles.
  • First aid (overview): If inhaled—move to fresh air; if on skin—wash with soap and water; if in eyes—rinse cautiously with water for several minutes; if ingested—rinse mouth. Seek medical attention if symptoms persist.
  • Spill/cleanup: Avoid dust formation; collect by gentle sweeping or damp wipe and dispose according to institutional guidelines.
  • Always consult the SDS for definitive hazard, exposure limits, and emergency measures.

Solvent Selection

• Peptide polarity and solvation (general):

  • GPLGIAGQ contains predominantly nonpolar residues (Leu, Ile, Ala) and multiple Gly, with one polar Gln. As a free acid with a protonated N-terminus (in TFA salt), it is amphiphilic but can be moderately hydrophobic.

• Recommended solvents (literature guidance):

  • Primary choices: Water, PBS, or other neutral buffers for assays where the peptide is adequately soluble.
  • Co-solvent strategy: If insoluble in pure water, dissolve first in a minimal volume of DMSO (or 10–50% acetonitrile/water with 0.1% formic or acetic acid), then dilute into aqueous buffer to the working concentration, keeping final DMSO ≤1–2% for cell-based work.
  • pH adjustment: Slight basification (e.g., 10–20 mM HEPES or Tris at pH 7.5–8.0) can aid dissolution by deprotonating the C-terminus while keeping the N-terminus largely protonated.

• Miscibility and compatibility (general):

  • DMSO and water are fully miscible; acetonitrile-water mixtures are common for RP-HPLC manipulations.
  • Avoid prolonged exposure to high pH (>9) which may catalyze backbone cleavage or deamidation (especially at Gln).

• Comparison (contextual):

  • Water vs DMSO: Water is preferred for biological assays; DMSO is a powerful cosolvent for initial dissolution. Methanol/ethanol are less preferred due to denaturing effects in some bioassays.
  • TFA-containing solutions are acidic; if acid-sensitive applications are planned, exchange TFA for acetate and/or neutralize post-dissolution.

Storage and Reconstitution

• Item-specific (from Product Data):

  • Storage: Store at −20°C, desiccated.
  • Shipping: Ice chest with ice pads.

• Reconstitution (general guidance for peptides; not a specification):

  • Equilibrate the sealed vial to room temperature in a desiccator before opening to prevent moisture condensation.
  • Dissolve initially in sterile water or a small volume of DMSO if aqueous solubility is limited, then dilute with the desired buffer. If the TFA counterion lowers pH excessively, adjust to neutral with base or perform counterion exchange to acetate if needed.
  • Working stocks: 1–10 mM (or as required by assay); filter sterilize (0.22 µm) for cell-based work.
  • Aliquoting: Prepare single-use aliquots to avoid freeze–thaw cycles. Store aliquots at −20°C or below. For long-term storage, −80°C is often beneficial.
  • Stability: Protect from light if labeled with chromophores (not part of this item). Avoid repeated warming; thaw on ice and use promptly. Aqueous solutions are generally most stable for hours to days at 2–8°C depending on buffer; assess by LC–MS where critical.

• Disposal: Follow institutional guidelines. Peptide solutions containing TFA should be collected as halogenated aqueous waste where required.

• Research Use: For research use only.

Structure and Identity

Brief description: GPLGIAGQ TFA is an octapeptide with the sequence Gly–Pro–Leu–Gly–Ile–Ala–Gly–Gln, supplied as its trifluoroacetate (TFA) salt.

• Item-specific (from Product Data):

  • SKU: G658993
  • Product name: GPLGIAGQ TFA
  • CAS: 109053-09-0 (free peptide)
  • Storage: Store at −20°C, desiccated; shipped on ice with ice pads.
  • SMILES: Not specified for this item; refer to CoA/Spec Sheet.
  • InChIKey: 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.

• Computed/literature (for the free peptide, neutral form; indicative only):

  • Sequence: H–Gly–Pro–Leu–Gly–Ile–Ala–Gly–Gln–OH (N-terminus free amine; C-terminus carboxylate).
  • Monoisotopic mass (free peptide): ~711.39 Da (literature calculation from residue masses).
  • Average mass (free peptide): ~711.81 Da (literature calculation).
  • Note: TFA salts commonly contain ~1 equiv trifluoroacetate per basic site (literature), which increases the total formula mass; actual counterion content may vary by lot. Consult CoA for exact salt content.

• Structural features (general description):

  • Linear, unmodified L-peptide with three Gly residues providing flexibility; one Pro imposing a β-turn tendency; branched hydrophobic residues Leu and Ile; small Ala; polar amide Gln at C-terminus vicinity.
  • Functional groups: one primary amine (N-terminus), one terminal carboxylic acid, multiple backbone amide bonds, one side-chain amide (Gln). No disulfides or aromatic residues.
  • Stereochemistry: Typically supplied as all-L amino acids (literature norm for synthetic bioactive peptide motifs).

Synthetic Utility

• Functional groups available for derivatization:

  • N-terminus: Primary amine for acylation (e.g., fluorophores, biotin), carbamylation, or coupling to carriers (e.g., NHS esters).
  • C-terminus: Carboxyl group for amide formation (e.g., coupling to amines, resin attachment, or conversion to amide to modulate solubility/stability).
  • Side chains: Gln amide is typically non-reactive under mild conditions but can be targeted in specialized chemistries; Pro, Leu, Ile, Ala, Gly lack nucleophilic side chains, simplifying selective end-labeling strategies.

• Roles in synthesis (literature):

  • Building block for FRET substrates: Install a donor at the N-terminus and a quencher at the C-terminus (or vice versa) via standard amide couplings (HATU/HBTU/EDC·Oxyma) to create protease-responsive probes.
  • Spacer/linker in conjugation: Insert between a targeting ligand and a payload to impart MMP-responsiveness. Add flexible spacers (Ahx/PEG) to tune accessibility.
  • Solid-phase transformations: Sequence can be assembled or extended on resin (Fmoc/tBu strategy) to introduce additional recognition elements or handles (e.g., azide/alkyne for click chemistry via N-terminal modification).

• Retrosynthetic value:

  • The absence of nucleophilic side chains reduces protecting group complexity; selective, orthogonal end-functionalization is straightforward.
  • For orthogonal dual labeling, temporarily protect one terminus (e.g., Boc/Alloc on N-terminus, methyl/allyl ester at C-terminus) while modifying the other, then deprotect under orthogonal conditions.

Target Specificity

Not applicable. This product is a synthetic peptide, not an antibody or biological affinity reagent. No antigen/epitope, clone, isotype, or species reactivity information applies.

Domande frequenti

What is the purity of this product?

This product is supplied at ≥99% purity (chemical assay). Lot-specific values are stated on the Certificate of Analysis.

How should this product be stored?

Store at ?20 °C, desiccated. Keep the container tightly closed with desiccant — the material is moisture-sensitive.

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 109053-09-0(free), the molecular formula is C31H53N9O10(free), and the molecular weight is 711.8(free) g/mol.

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.