FPYVAE peptide, Inhibitor of hydroxymethylglutaryl-CoA reductase, CAS No.rp174038, Inhibitor of hydroxymethylglutaryl-CoA reductase

CAS: rp174038 Cat. No.: rp174038 PubChem CID: 46906163
Disponibile su ordine
QUALITÀ & PUREZZA Moligand™ ? Moligand™ — Aladdin's line of ligands and bioactive small molecules. Use for receptor, pathway, and binding studies needing defined small-molecule tools.
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Dimensione
Germania (EU)
USA*
Prezzo
Qtà
500μg
rp174038-500μg
Su ordinazione · 8–12 settimane
2.082,49€
1mg
rp174038-1mg
Su ordinazione · 8–12 settimane
3.470,87€
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Specifiche

Product Name
FPYVAE peptide, Inhibitor of hydroxymethylglutaryl-CoA reductase, CAS No.rp174038
Grado
Moligand™
Specifiche e purezza
Moligand™
Tipo di azione
INHIBITOR
Meccanismo d'azione
Inhibitor of hydroxymethylglutaryl-CoA reductase
CAS
rp174038
Tipo di molecola
Proteine
Product Line
Prodotti biologici
Stoccaggio e spedizione
Condizioni di conservazione di stoccaggio
Room temperature

Dati avanzati

Taxonomic Classification

Taxonomy Tree

KingdomOrganic compounds
SuperclassOrganic acids and derivatives
ClasseCarboxylic acids and derivatives
SubclassAmino acids, peptides, and analogues
Intermediate Tree Nodes Peptides
Direct ParentOligopeptides
Alternative Parents Tyrosine and derivatives  Phenylalanine and derivatives  Glutamic acid and derivatives  Valine and derivatives  Proline and derivatives  N-acyl-L-alpha-amino acids  Alpha amino acid amides  Alanine and derivatives  Amphetamines and derivatives  Pyrrolidinecarboxamides  N-acylpyrrolidines  1-hydroxy-2-unsubstituted benzenoids  Aralkylamines  Dicarboxylic acids and derivatives  N-acyl amines  Tertiary carboxylic acid amides  Secondary carboxylic acid amides  Amino acids  Carboxylic acids  Azacyclic compounds  Organic oxides  Hydrocarbon derivatives  Carbonyl compounds  Monoalkylamines  
Molecular FrameworkAromatic heteromonocyclic compounds
Substituents Alpha-oligopeptide - Tyrosine or derivatives - Phenylalanine or derivatives - Glutamic acid or derivatives - N-acyl-alpha amino acid or derivatives - N-acyl-l-alpha-amino acid - N-acyl-alpha-amino acid - Proline or derivatives - Valine or derivatives - Alpha-amino acid amide - Alanine or derivatives - Amphetamine or derivatives - N-substituted-alpha-amino acid - Alpha-amino acid or derivatives - Pyrrolidine carboxylic acid or derivatives - Pyrrolidine-2-carboxamide - N-acylpyrrolidine - Phenol - 1-hydroxy-2-unsubstituted benzenoid - Aralkylamine - Monocyclic benzene moiety - Dicarboxylic acid or derivatives - Fatty amide - N-acyl-amine - Fatty acyl - Benzenoid - Pyrrolidine - Tertiary carboxylic acid amide - Secondary carboxylic acid amide - Amino acid or derivatives - Amino acid - Carboxamide group - Azacycle - Organoheterocyclic compound - Carboxylic acid - Organooxygen compound - Amine - Carbonyl group - Organic nitrogen compound - Organonitrogen compound - Primary amine - Hydrocarbon derivative - Organic oxygen compound - Organic oxide - Primary aliphatic amine - Aromatic heteromonocyclic compound
DescrizioneThis compound belongs to the class of organic compounds known as oligopeptides. These are organic compounds containing a sequence of between three and ten alpha-amino acids joined by peptide bonds.
External Descriptors Not available
Struttura 3D
Modello di struttura chimica interattiva





Obiettivi associati (umani)
HMGCR Tclin 3-hydroxy-3-methylglutaryl-coenzyme A reductase (0 Activities)
Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)
Meccanismi d'azione
Certificati (CoA, COO, BSE/TSE e tabella di analisi)
C of A & Other Certificates(BSE/TSE, COO):
Analytical Chart:
Informazioni genetiche
Reference
  • 1. Kinetics and inhibition of recombinant human cystathionine gamma-lyase. Toward the rational control of transsulfuration., The Journal of biological chemistry, Steegborn, C C and 7 more authors.
  • 2. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences., Proceedings of the National Academy of Sciences of the United States of America, Strausberg, Robert L RL and 83 more authors.
  • 3. Genomic basis of cystathioninuria (MIM 219500) revealed by multiple mutations in cystathionine gamma-lyase (CTH)., Human genetics, Wang, Jian J and Hegele, Robert A RA.
  • 4. Cloning and nucleotide sequence of human liver cDNA encoding for cystathionine gamma-lyase., Biochemical and biophysical research communications, Lu, Y Y, O'Dowd, B F BF, Orrego, H H and Israel, Y Y.
  • 5. Single nucleotide polymorphism in CTH associated with variation in plasma homocysteine concentration., Clinical genetics, Wang, J J, Huff, A M AM, Spence, J D JD and Hegele, R A RA.
  • 6. Cystathionine gamma-lyase overexpression inhibits cell proliferation via a H2S-dependent modulation of ERK1/2 phosphorylation and p21Cip/WAK-1., The Journal of biological chemistry, Yang, Guangdong G, Cao, Kun K, Wu, Lingyun L and Wang, Rui R.
  • 7. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)., Genome research, Gerhard, Daniela S DS and 115 more authors.
  • 8. Towards a proteome-scale map of the human protein-protein interaction network., Nature, Rual, Jean-François JF and 37 more authors.
  • 9. The DNA sequence and biological annotation of human chromosome 1., Nature, Gregory, S G SG and 178 more authors.
  • 10. Polymorphisms in one-carbon metabolism and trans-sulfuration pathway genes and susceptibility to bladder cancer., International journal of cancer, Moore, Lee E LE and 14 more authors. more
Calcolatori di soluzioni
Recensioni

Recensioni dei clienti

Application Protocols

No tested/validated application protocols are provided for this product. The following are general, non-item-specific protocol outlines to aid initial use; adjust to your platform and validate empirically.

  1. Preparation of peptide stock solutions (general):
  • Warm buffer to room temperature. If needed, wet peptide with minimal DMSO or ACN, then add buffer to reach 1–10 mM. Vortex and sonicate briefly if necessary. Filter through 0.22 µm low-binding membrane if sterility is required. Aliquot and store appropriately.
  1. Surface plasmon resonance (SPR) ligand screening (general):
  • Immobilize protein on CM5 chip via amine coupling (pH scouting recommended). Inject peptide series (0.1–100 µM) in HEPES-buffered saline with 0.005–0.05% surfactant. Include reference channel and blank injections. Fit 1:1 or steady-state models as appropriate.
  1. LC–MS identity check (general):
  • RP-HPLC C18, linear gradient 5–60% ACN in 0.1% formic acid over 10–20 min. ESI+ MS scan m/z 200–2000. Confirm charge-state envelope and deconvoluted mass against theoretical value (obtain from CoA or sequence calculation).
  1. Enzymatic stability assay (general):
  • Incubate peptide (10–50 µM) with protease or serum at 37 °C. Quench at time points with ACN + 0.1% FA. Analyze by LC–MS to assess degradation.

Item-specific parameters (concentration ranges, solvent percentages, chip chemistry, extinction coefficients): Not specified for this item; refer to CoA/Spec Sheet and optimize locally.

Biological Roles

No biological role is assigned to this specific synthetic hexapeptide. The following context frames how a sequence like FPYVAE may behave in biochemical systems (general knowledge; not a claim of endogenous function).

Sequence-driven properties (general):

  • Aromatic interaction potential: Phe and Tyr enable π–π and cation–π interactions; Tyr’s phenolic OH can H-bond or participate in redox chemistry (at elevated pH or in enzymatic contexts).
  • Conformational features: Proline at position 2 introduces a backbone kink and can exist in cis/trans conformers, influencing recognition by peptidyl–prolyl isomerases and binding landscapes.
  • Charge/hydrophobic balance: With a terminal Glu and the peptide termini, the net charge near neutral pH typically trends around −1, moderating solubility and interaction with basic protein patches.

Potential research contexts:

  • Model ligand for SH3/WW-like domains (aromatic/proline-rich recognition) or acidic-tail binding sites; suitability must be determined experimentally.
  • Minimal motif for studying aromatic–hydrophobic cluster recognition in protein–peptide interactions.
  • UV-active reporter: Tyr and Phe facilitate A280-based tracking in chromatography and binding assays.

Caveats:

  • No endogenous pathway attribution, receptor specificity, or biological activity is established for this item.
  • Any observed activity in assays should be validated with orthogonal controls (scrambled sequences, single-point mutants) to rule out aggregation or nonspecific binding.

All uses are for laboratory research only; not for diagnostic or therapeutic use.

Buffer Applications

As a short peptide, FPYVAE is typically handled in aqueous buffers. Item-specific buffer recommendations are not provided; the following are general, practical guidelines for stock preparation and assay use.

Common buffer systems (general):

  • PBS (pH 7.2–7.4): Routine handling and bioassays; add 0.01–0.1% carrier protein (e.g., BSA) only if adsorption to labware is a concern and is compatible with your assay.
  • HEPES (10–50 mM, pH 7.0–8.0): Low temperature/pH drift; useful for biophysical methods and cell-free assays.
  • Tris (10–50 mM, pH 7.5–8.0): Good buffering near neutral to slightly basic pH; avoid for UV-quantitation accuracy if relying on precise extinction coefficients.
  • Acetate or phosphate (pH 5.0–7.0): If increased protonation is needed for solubility; monitor for potential aggregation near the isoelectric region.

Practical tips:

  • Stock preparation: Aim for 1–10 mM stocks. If solubility is limited, dissolve in minimal DMSO (or 10–30% ACN), then dilute into buffer with vigorous mixing.
  • Filters: Use low-protein-binding filters (PVDF or PES) if sterile filtration is required.
  • Adsorption control: Use siliconized tubes or add inert carriers for very dilute solutions.
  • Stability: Avoid repeated freeze–thaw cycles of solutions; aliquot and store at ≤−20 °C for long-term solution stability (see Storage & Reconstitution).

Item-specific buffer compatibility and stability: Not specified for this item; consult CoA/SDS and validate empirically for your assay conditions.

Green Alternatives

Peptide handling is inherently more aqueous than small-molecule chemistry, enabling greener solvent choices. For FPYVAE, prioritize water-based systems, adding small amounts of benign co-solvents only as necessary.

Greener choices (general guidance):

  • Primary medium: Water and buffered aqueous media (PBS, HEPES, citrate/phosphate) at near-neutral pH.
  • Co-solvents hierarchy:
    • Preferred: Ethanol (EtOH) for limited co-solvation in biocompatible assays where appropriate.
    • Acceptable with care: Acetonitrile (ACN), widely used in LC–MS/HPLC; volatile and recoverable.
    • Use sparingly: DMSO—effective but with higher environmental persistence; keep ≤1–2% v/v in working solutions.
  • Solid-phase synthesis (SPPS) context: If preparing analogs, consider greener process adaptations—e.g., replacing DMF with NBP/PC (n-butylpyrrolidone/propylene carbonate) or using green coupling reagents (literature) while validating quality. This is general process guidance and not specific to the supplied item.

Comparison (general; qualitative):

  • Water/buffer: Lowest EHS footprint; maximal assay compatibility.
  • EtOH vs DMSO: EtOH is greener and more biodegradable; DMSO is a stronger solvent but should be minimized.
  • ACN vs MeOH: ACN offers lower viscosity and is standard for peptide LC; MeOH is more toxic than EtOH but acceptable in low percentages.

Waste minimization:

  • Prepare concentrated stocks, aliquot to reduce freeze–thaw waste, and avoid over-preparation that leads to disposal.
  • Use LC gradients optimized to shorten runs and reduce solvent consumption.

Item-specific environmental attributes: Not specified for this item; refer to SDS and institutional green-chemistry policies.

Pharmaceutical Uses

No pharmacopeial status or excipient role is provided for this item. The product is for research use only. The following points summarize general, non-clinical contexts in which short peptides are employed during pharmaceutical R&D workflows (not specific to this item):

  • Screening reagents: Use in biochemical/biophysical assays to identify binding partners, measure structure–activity relationships (SAR), or benchmark assay performance.
  • Analytical standards: Reference materials for method development in LC–MS peptide analytics (retention behavior, ionization efficiency) due to the presence of UV-active Tyr/Phe.
  • Formulation research (preclinical): Model compounds for studying peptide solubilization, adsorption to packaging, and stability in various buffers.
  • Conjugation method development: Testbeds for coupling chemistries (e.g., NHS ester, click chemistry after azido/alkynyl derivatization) and linker stability.

Exclusions and caveats:

  • No claims are made regarding therapeutic use, diagnostic utility, GMP grade, or compliance with pharmacopeial monographs for this item.
  • If translation toward regulated studies is intended, procure GMP-grade material and full quality documentation, and perform suitability assessments per ICH Q-series guidelines.

Item-specific pharmaceutical application data: Not specified for this item; refer to CoA/Spec Sheet and internal validation.

Physical Properties

Item-specific numerical specifications have not been provided for this peptide. The following guidance distinguishes between unspecified values and general, sequence-based expectations useful for planning.

Item-specific specs:

  • Appearance: 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.
  • Water content, residual solvents, purity format: Not specified for this item; refer to CoA/Spec Sheet.

Sequence-based/literature expectations (general guidance for FPYVAE):

  • Physical state: Typically a white to off-white amorphous solid or lyophilized powder (literature, common for short peptides).
  • Solubility (qualitative): Mixed character. Hydrophobic residues (F, Y, V) may reduce aqueous solubility, while E and termini enhance it. Often soluble in water or aqueous buffers at neutral to slightly basic pH; if limited, dissolve first in a small volume of DMSO or 10–30% acetonitrile, then dilute with buffer (general peptide practice).
  • Charge state (theoretical): At pH ~7.4, net charge commonly ~−1 due to deprotonated Glu side chain and C-terminus, with protonated N-terminus (sequence-based calculation; confirm experimentally).
  • pI, logP, refractive index, BP/MP: Not typically defined/used for peptides of this size; not available.

Practical notes:

  • For accurate mass confirmation (e.g., LC–MS), request or consult the CoA for exact sequence, counterions (e.g., TFA, acetate), and measured MW. Counterions and salt forms can shift apparent mass and solubility.
Quality and Grades
  • Grade/Purity: Moligand™ (as provided).

What Moligand™ implies (general description):

  • Moligand™ denotes inclusion in a curated small-molecule/ligand discovery collection designed for screening, target engagement studies, or chemoproteomics. For peptides, this typically emphasizes sequence-defined identity and suitability for library screening rather than pharmacopeial compliance.

Item-specific quality not specified:

  • Purity level, counterion content (e.g., TFA vs acetate), residual solvents, water content, metal content, endotoxin/bioburden: Not specified for this item; refer to CoA/Spec Sheet.

Analytical characterization commonly expected for research peptides (general):

  • Identity confirmation by LC–MS (electrospray), with observed mass matching the calculated [M+H]+ within instrument tolerance.
  • Purity assessed by analytical RP-HPLC at 214/220 nm and 254/280 nm (peptide bond and aromatic absorption). Typical library-grade materials target >90% by HPLC, but the exact threshold for this item is not specified.
  • Counterion determination by ion chromatography or NMR where relevant.

Implications for use:

  • For biochemical assays, verify purity and counterion on the CoA to adjust concentrations (counterions add mass) and to anticipate UV absorbance (Tyr and Phe absorb near 280 nm/257 nm).
  • If orthogonal methods (HRMS, amino acid analysis, Edman sequencing) are required for regulated workflows, request supporting documentation prior to use.

Bottom line: Use the CoA/Spec Sheet accompanying your lot to confirm assay-suitable quality attributes for FPYVAE.

Reaction and Applications

Given its inclusion in a Moligand™ discovery collection, FPYVAE peptide can serve as a modular ligand or probe in early-stage screening and chemical biology. While no application claims are specified for this item, the sequence suggests several practical research uses.

Representative application domains (general for short peptides):

  • Ligand discovery and target deconvolution: Use as a peptide ligand in affinity selection–mass spectrometry (AS–MS) or SPR/BLI to identify protein binders or map binding preferences for hydrophobic pockets engaging aromatic residues.
  • Epitope/motif mapping: The FPY motif is aromatic-rich; such hexamers are often included in positional scanning libraries to assess binding contributions of Phe/Tyr and a terminal acidic group (E) to protein interfaces.
  • Enzymology: Substrate or inhibitor leads for peptidases/peptidyl–prolyl isomerases (PPIases) where Pro at position 2 can modulate cis–trans isomerization kinetics.
  • Materials/assembly studies: Short amphiphilic peptides can self-associate; monitor aggregation by CD/DLS under varying ionic strength and pH.

Experimental notes:

  • Quantification: Tyr enables A280 measurement (literature ε280 ~1490 M−1 cm−1 for Tyr; Phe contributes modestly). Correct for buffer baseline and counterions.
  • Immobilization: N-terminus or side chains can be functionalized (e.g., NHS–ester coupling) for surface display; confirm that any modification sites do not disrupt intended interactions.
  • Controls: Include scrambled or alanine-scan variants to deconvolute sequence-specific effects.

Item-specific validated applications: Not specified for this item; design studies according to your platform and confirm performance empirically.

Reaction Conditions

No reaction or assay conditions are specified for this catalog item. The following are general, literature-derived conditions relevant to short peptide handling and derivatization; adapt to your system and validate empirically.

  • Stock solution preparation (general):

    • Dissolve to 1–10 mM in water or buffer (pH 7–8). If insoluble, wet with DMSO (up to 100 mM), then dilute to working strength keeping final DMSO ≤1–2% v/v.
    • For UV quantitation at 280 nm, use buffers with minimal background and correct for pathlength.
  • Conjugation (N-terminus acylation):

    • Reagents: NHS esters (e.g., biotin-NHS, succinimidyl esters of fluorophores).
    • Conditions: pH 7.5–8.5 in phosphate/borate buffer; 1.1–5 eq reagent; 15–120 min at RT. Quench with Tris or ethanolamine.
  • Phenolic modification (Tyr):

    • Diazonium coupling (literature): Azo coupling under mildly basic conditions (pH 8–9) with freshly generated aryl diazonium salts; monitor to avoid over-modification.
    • Enzymatic labeling: Tyrosinase-mediated coupling under aqueous conditions (pH ~7).
  • Side-chain carboxyl coupling (Glu):

    • Carbodiimide chemistry (EDC/NHS) in MES buffer pH 5.0–6.0; 1–2 h at RT for forming amide linkages to amines on surfaces or polymers.
  • Analytical LC–MS (typical peptide setup):

    • RP-HPLC: C18, 0.1% formic acid in water (A) / acetonitrile (B), 5–60% B over 5–30 min, 0.2–1 mL/min depending on column; detect at 214/220 nm and 280 nm.

Expected yields, times, and exact parameters will vary with scale, reagent quality, and substrate context; optimize and consult primary literature.

Safety and Handling

Safety details specific to this catalog item have not been provided. Always consult the product SDS for authoritative information.

Provided hazard information:

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

General safety considerations for synthetic research peptides:

  • Expected hazards: Low volatility, low acute toxicity by inhalation relative to small organic solvents; avoid inhalation of powders and contact with eyes/skin. Some peptides may cause irritation or allergic sensitization upon repeated exposure.
  • PPE: Laboratory coat, safety glasses, and appropriate gloves (e.g., nitrile). Use a dust mask or work in a fume hood/biological safety cabinet when weighing powders to minimize aerosolization.
  • Handling: Avoid generating dust. Use clean, dry spatulas. If reconstituting, use sterile technique when sterility is required. Clearly label aliquots with concentration, buffer, and date.
  • Storage incompatibilities: Strong oxidizers; proteases (avoid contamination that could degrade peptide). Keep away from moisture until reconstitution.
  • First aid (overview; consult SDS):
    • Inhalation: Move to fresh air; seek medical attention if symptoms persist.
    • Skin/eye contact: Rinse with water for 15 minutes; remove contaminated clothing; seek medical advice if irritation continues.
    • Ingestion: Rinse mouth; do not induce vomiting; seek medical advice.
  • Spill/cleanup: Avoid dust formation. Gently sweep up or use HEPA-filtered vacuum; dispose according to institutional guidelines.
  • Waste: Dispose as non-halogenated organic/biological laboratory waste per local regulations.

Note: For research use only; not for human or veterinary use.

Solvent Selection

Peptides require solvent strategies based on sequence hydrophobicity and ionizable groups. FPYVAE combines hydrophobic aromatics (F, Y), aliphatic residues (V, A), and an acidic residue (E), yielding mixed polarity and a modest net negative charge near neutral pH.

Primary solvents/buffers (general guidance):

  • Water or aqueous buffers (PBS, HEPES, Tris): Often adequate at pH 7–8; the deprotonated Glu and termini aid solubility. Adjust ionic strength to minimize self-association if needed.
  • Alkaline conditions: Slightly basic pH (8–9) can enhance solubility by deprotonating acidic groups; avoid prolonged exposure at high pH to limit base-catalyzed hydrolysis.
  • Co-solvents: If aqueous solubility is limited, pre-dissolve in minimal DMSO or 10–30% acetonitrile (ACN), then dilute into buffer. DMSO should be kept as low as assay tolerates (≤1–2% v/v in final solutions).
  • Denaturants (for stubborn cases): 1–2 M urea or low % SDS can aid solubilization for specific biophysical workflows; ensure compatibility with downstream assays.

Selection tips:

  • Aromatic content suggests moderate UV absorbance (Tyr, Phe). For UV-based quantification, choose solvents/buffers with minimal background at 280 nm; avoid Tris for precise absorbance if using extinction coefficients.
  • Avoid strong acids/bases unless required; phenolic Tyr can ionize at high pH (pKa ~10, literature), altering properties.

Comparison (general):

  • Water/buffer: Greenest, assay-friendly.
  • DMSO: Powerful co-solvent; minimize in bioassays.
  • ACN (with 0.1% TFA for HPLC): Excellent for analytical work; for stocks, exchange to volatile acid salts as needed.

Item-specific solubility data: Not specified for this item; verify empirically and consult the CoA.

Storage and Reconstitution

Storage conditions provided for this item: Room temperature (as supplied).

General best practices for peptides (complementary guidance):

  • Solid storage: Keep tightly sealed, desiccated, and protected from light. Although room temperature storage is indicated, long-term stability of peptides as solids is often enhanced at 2–8 °C or −20 °C; choose conditions consistent with your stability requirements and institutional policy.
  • Moisture control: Minimize exposure to ambient humidity; allow vials to warm to room temperature before opening to avoid condensation.

Reconstitution (general guidance; item-specific solvent not specified):

  • Initial dissolution: Start with water or buffer at pH 7–8. If solubility is limited, dissolve in minimal DMSO or 10–30% acetonitrile, then dilute with buffer.
  • Concentration: Prepare concentrated stocks (e.g., 1–10 mM) to limit solvent volume in assays. Determine exact concentration by UV at 280 nm (Tyr-containing) or by amino acid analysis; consult CoA for extinction coefficients if provided.
  • Aliquoting: Dispense single-use aliquots to avoid repeated freeze–thaw of solutions.

Solution storage (general):

  • Short term (hours–days): 2–8 °C.
  • Long term (weeks–months): ≤−20 °C or −80 °C recommended for aqueous stocks; avoid repeated thawing.
  • Avoid prolonged exposure to strong light and extreme pH.

Shipping: Not specified for this item.

Any item-specific stability data (e.g., shelf life, counterion, recommended diluent): Not specified for this item; refer to CoA/Spec Sheet.

Note: For research use only.

Structure and Identity

Short description: FPYVAE peptide is a hexapeptide composed of the L-amino-acid sequence Phe–Pro–Tyr–Val–Ala–Glu.

  • SKU: rp174038
  • Product name: FPYVAE peptide (sequence: FPYVAE)
  • Category: Small molecules and compound libraries (Moligand™ collection)
  • CAS: rp174038 (catalog identifier format; not a registry number)
  • PubChem CID: 46906163 (as provided)
  • InChIKey: 299546 (as provided)
  • SMILES: Not specified for this item; refer to CoA/Spec Sheet.

Structural features (general, sequence-based):

  • Residue composition: F (aromatic, hydrophobic), P (conformationally constrained), Y (phenolic aromatic), V (aliphatic hydrophobic), A (small aliphatic), E (acidic, anionic at neutral pH).
  • Functional groups: peptide backbone (amide bonds), phenyl rings (F, Y), phenolic OH (Y), carboxylate side chain (E), terminal amino (N-terminus) and carboxyl (C-terminus) groups.
  • Stereochemistry: Typically L-configuration for each residue in synthetic research peptides unless otherwise stated (item-specific stereochemical specifications are not provided; verify on CoA).
  • 2D description (in words): Linear hexapeptide with an N-terminal phenylalanine linked via successive trans amide bonds to proline (introducing a backbone kink), tyrosine (bearing a para-phenolic OH), valine and alanine (aliphatic), and a C-terminal glutamate side chain terminating in a γ-carboxyl group.

Identity notes:

  • Molecular formula and molecular weight: Not specified for this item; refer to CoA/Spec Sheet. Sequence-based theoretical values can be computed if needed for method development (see Physical Properties).
Synthetic Utility

FPYVAE is a sequence-defined hexapeptide that can serve as a building block, ligand, or reference in synthesis and chemical biology.

Utility in synthesis (general):

  • Scaffold for diversification: The peptide presents multiple functional handles—N-terminus, C-terminus, Tyr phenol, Glu side-chain carboxyl—for orthogonal modification (acylation, alkylation/arylation after protection, ester/amide formation).
  • Conjugation anchor: Install biotin, fluorophores, affinity tags, or linkers via NHS ester coupling to the N-terminus or lysine-like surrogates introduced synthetically (e.g., add-on residues or click handles at either terminus).
  • Macrocyclization precursors: Head-to-tail or side-chain-to-terminus cyclization can be explored to modulate conformation and proteolytic stability; Tyr can participate in oxidative coupling strategies (literature: tyrosine click/oxidative dityrosine formation under controlled conditions).
  • Peptidomimetic development: Use as a parent sequence for alanine scanning, D-amino acid substitution, N-methylation of backbone amides, or replacement of Tyr/Phe with non-natural aromatics to tune binding and permeability.

SPPS context (if preparing analogs; general):

  • Fmoc/tBu strategy with standard couplings (e.g., HATU/HOAt or Oxyma/DIC) delivers sequences of this length efficiently. Proline and valine may require optimized activation to avoid racemization.
  • Protecting groups: Tyr(tBu) for phenol; Glu(OtBu) for side chain. Final TFA cleavage yields the free acid; counterion will often be TFA unless exchanged.

Item-specific synthetic details (grade, protecting groups, counterion): Not specified for this item; refer to CoA/Spec Sheet.

Target Specificity

Target specificity data (e.g., protein target, receptor, antigen, binding constants) are not provided for this item.

  • Validated targets: Not specified for this item; refer to CoA/Spec Sheet.
  • Binding affinity/kinetics: Not specified for this item; refer to CoA/Spec Sheet.
  • Species reactivity or epitope information: Not applicable; this product is a synthetic peptide without assigned immunological specificity in the provided data.

Guidance for users:

  • If employing FPYVAE in binding studies, determine specificity empirically using appropriate negative controls (scrambled sequence, alanine-scan variants) and orthogonal methods (SPR/BLI/ITC/AS–MS).
  • Report any derived specificity as assay- and condition-dependent, including buffer composition, temperature, and immobilization strategy.

Domande frequenti

How should this product be stored?
Store at room temperature.
What are the CAS number, molecular formula and molecular weight?
The CAS Number is rp174038. InChIKey QKSOHTFYHNYHRK-YFVDCHTDSA-N.
What is Moligand??
Moligand? is one of Aladdin Scientific's premium product lines, formulated for high-purity applications across multiple workflows. Compared to standard grades in the same workflow, Moligand? products typically offer tighter specifications, more rigorous QC, and stronger lot-to-lot consistency.
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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