d-KYFIL , CAS No.D1442359

CAS: D1442359 Cat. No.: D1442359 Summenformel: C₃₆H₅₅N₇O₆ Molekulargewicht: 681.87

Storage

Store at -20°C

Shipped In

Ice chest + Ice pads

Übersicht

d-KYFIL is a peptide-based biomaterial that can be used for stereocomplexation and can be used to study the regulation of supramolecular assembly of hydrogel biomaterials.

Specifications

Storage

Store at -20°C

Verschickt in

Ice chest + Ice pads

Dieses Produkt erfordert Kühlkettenversand. Grundversand und andere Economy-Optionen sind nicht verfügbar.

Namen und Kennungen

• Molekulargewicht: 681.87

Application Protocols

Item-specific validated protocols and dilutions: Not specified for this item; refer to CoA/Spec Sheet.

General protocols for peptide use (literature/general):

• Preparing stock solutions: Allow vial to warm in a desiccator to room temperature. Briefly centrifuge to collect material. Dissolve using the strategy in Solvent Selection. Filter (0.22 µm) if sterility is required. Aliquot and store at −20°C.
• Concentration determination: If an extinction coefficient is known or computed from sequence (Tyr/Phe contribute), quantify by UV at 280/257 nm with appropriate blank. Alternatively, weigh accurately and correct for net peptide content from the CoA; confirm by LC–MS if critical.
• Conjugation to NHS-activated dyes: Dissolve peptide in 50 mM sodium bicarbonate, pH ~8.3. Add dye (3–10 eq). React 1 h at room temperature in the dark. Quench with ethanolamine. Purify by RP-HPLC. Verify labeling by MS.
• LC–MS system suitability (example workflow): Prepare 5–50 µM solutions in 0.1% formic acid in water/acetonitrile. Inject onto C18 gradient. Record retention and MS response to benchmark instrument performance. Adjust concentrations to your detector’s linear range. Adapt all steps to your application and instrument; validate conditions locally.

Biological Roles

Item-specific biological role or target: Not specified for this item; refer to CoA/Spec Sheet.

General context for short peptides (literature/general):

• Peptides can mimic protein segments, act as substrates/inhibitors in enzyme studies, or serve as ligands in receptor-binding assays. The inclusion of a D-amino acid often modulates conformation, receptor interaction, and proteolytic stability compared with the all-L counterpart.
• Side-chain functionalities present in a KYFIL motif suggest potential for hydrophobic and aromatic interactions (Phe/Tyr) and electrostatic contacts via Lys. Tyr’s phenolic OH can participate in hydrogen bonding and may influence redox behavior under oxidative conditions.
• In cellular studies, sequence- and context-dependent uptake may occur, but there is no item-specific data here; any biological activity should be established empirically under controlled research conditions.
• Analytical biology: Such peptides are commonly used as calibration standards or to validate sample preparation, digestion efficiency, and LC–MS/MS method performance in proteomics workflows. Caution: No clinical or therapeutic claims are made. This product is for research use only (per Product Data). Any biological function or activity must be determined by the end user in their specific system.

Buffer Applications

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

General buffer guidance for peptide stock preparation (literature/general):

• Stock concentration: Prepare a concentrated stock (e.g., 1–10 mM, as assay permits) to minimize freeze–thaw. Determine exact concentration by UV, gravimetry corrected for net peptide content, or amino acid analysis.
• Dissolution workflow: 1) Wet the peptide with a minimal volume of water or DMSO (if hydrophobic), 2) Adjust pH slightly acidic (pH ~3–6) to protonate Lys and enhance solubility if needed, 3) Bring to final volume with buffer compatible with downstream experiments (e.g., PBS, HEPES, acetate).
• pH considerations: Avoid strong alkaline pH during storage to reduce base-catalyzed side reactions (e.g., deamidation, racemization). For Tyr-containing peptides, minimize prolonged exposure to oxidizing buffers.
• Filtration/sterility: If sterile stocks are needed, filter through a 0.22 µm low-binding membrane. Consider glass containers to limit adsorption for hydrophobic sequences.
• Additives: Small amounts of non-ionic surfactants (e.g., 0.01% Tween-20) can reduce surface adsorption in some assays; verify compatibility first. Note: Optimize buffer composition empirically based on your assay and the peptide’s observed solubility and stability profile.

Green Alternatives

Applicability: As a peptide reagent, the concept of a “greener alternative compound” is not directly relevant. However, greener handling and solvent choices can improve sustainability of workflows.

Greener practice recommendations (literature/general):

• Prefer aqueous buffers: Dissolve in water or lightly acidified water before using organic co-solvents.
• Minimize DMSO: If required for solubility, keep DMSO to the lowest concentration compatible with your assay and dispose of waste properly.
• Reduce single-use plastics: Hydrophobic peptides may adsorb to plastics; choosing glass vials can both reduce losses and waste from repeated transfers.
• Energy efficiency: Store at −20°C (per Product Data) and avoid unnecessary deep-cold storage; make concentrated aliquots to reduce freezer door openings and freeze–thaw cycles.

Comparison (general):

• Water/Buffer vs DMSO: Water has superior EHS profile; DMSO improves solubility but can affect biological systems and increase solvent load.
• Ethanol/Isopropanol vs Halogenated solvents: If a co-solvent is needed and assay-compatible, prefer lower-toxicity alcohols over chlorinated solvents (which are typically unnecessary for peptides). Note: No formulation or process substitutions are specified for this item; consult your EHS program for green chemistry metrics in your lab context.

Pharmaceutical Uses

No pharmaceutical or clinical use is claimed. This product is supplied strictly for research use only (per Product Data).

General formulation-related context for peptides (literature/general):

• Analytical standards: Short peptides are sometimes used as system suitability standards or reference materials in method development and QC for peptide drug manufacturing (outside of clinical contexts).
• Excipients: Not applicable to this item; no excipient role is specified.
• Delivery research: In preclinical research, peptides are formulated in aqueous buffers or with co-solvents for in vitro assays; excipient choices (e.g., mannitol, trehalose) may stabilize lyophilized materials, but the presence of such excipients for this item is not specified; refer to the CoA/Spec Sheet.
• Regulatory status: Not specified for this item; no pharmacopeial monograph is indicated. Any application towards human or veterinary use is not covered and is prohibited without appropriate approvals. End users must perform risk assessments and method validations for their specific research-only workflows.

Physical Properties

Item-specific data:

• Appearance: Not specified for this item; refer to CoA/Spec Sheet.
• Exact MP/BP, density, refractive index, pKa, logP/logD, and solubility: Not specified for this item; refer to CoA/Spec Sheet.

General properties for small peptides (literature/general):

• Physical state: Typically a white to off-white amorphous solid or lyophilized powder when supplied as a peptide.
• Melting/decomposition: Peptides usually decompose before boiling; melting points are not often meaningful due to degradation.
• Solubility behavior: Sequence-dependent. Basic residues (e.g., Lys) favor solubility in slightly acidic aqueous media; hydrophobic/aromatic residues (Tyr, Phe, Ile, Leu) can reduce solubility in neutral water, sometimes necessitating co-solvents (e.g., DMSO) or pH adjustment. Phenolic Tyr may participate in hydrogen bonding; Lys ε-amine is protonated under acidic conditions, enhancing water solubility.
• UV absorbance: Aromatic residues (Tyr, Phe) contribute to UV absorption near 257–280 nm (qualitative; exact ε depends on sequence and conditions). For quantification, determine extinction coefficient experimentally or compute from sequence (literature tools), then verify.
• Hygroscopicity: Many peptides are hygroscopic and may absorb moisture, which affects weighing accuracy and stability. Note: For any property required in specifications or method development, consult the product CoA/Spec Sheet and SDS.

Quality and Grades

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

General guidance for peptide quality (literature/general):

• Common peptide grades: Crude (minimal purification), Desalted, >70–90% (research grade), >95% (high purity), and >98–99% (analytical grade). Higher purity reduces interference in bioassays and conjugations, improves mass balance in quantitative studies, and decreases side-product peaks in HPLC.
• Characterization: Peptide identity and quality are typically verified by LC–MS (m/z profile), analytical HPLC (purity by area %), and where relevant, amino acid analysis or NMR. CoA usually includes sequence, counter-ion, net peptide content, purity, and analytical conditions.
• Counter-ions and content: Peptides isolated via TFA often contain TFA salt; others may be acetate or chloride salts. Net peptide content can differ from gross weight due to residual water and counter-ions; for quantitative work, adjust dosing to net peptide content (from CoA).
• Stabilizers: Not typically added unless specified. If present (e.g., mannitol/trehalose for lyophilizates), they will be listed on the CoA/Spec Sheet.
• Recommendation: For sensitive applications (e.g., receptor binding, enzymology), confirm purity specification, salt form, and net peptide content on the CoA for this specific lot.

Reaction and Applications

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

General research applications for short peptides (literature/general):

• Biochemistry and biophysics: Use as model peptides to probe hydrophobic interactions, aromatic stacking (Tyr/Phe), and the impact of a D-residue on secondary structure and proteolytic stability.
• Enzymology/proteolysis studies: Assess susceptibility to proteases; D-residue incorporation often confers resistance to common proteases, enabling stability studies.
• Conjugation chemistry: The ε-amine of Lys enables site-selective modification via NHS-esters, isocyanates, or activated carbonates; Tyr phenol can undergo diazonium coupling or electrophilic substitution under controlled conditions.
• Analytical standards: Serve as retention time or ionization-response standards in LC–MS method development for peptide analytics (sequence-dependent; verify on your platform).
• Materials/assembly: Short amphiphilic peptides can form aggregates or films; investigate sequence-driven self-assembly (requires empirical confirmation). Practical tips:
• Use freshly prepared solutions for bioassays. Filter if sterility is required. For conjugations, buffer at pH 7.5–8.5 for amine-NHS reactions and exclude competing primary amines.
• Validate concentration by UV if extinction coefficients are known; otherwise, use gravimetry corrected by net peptide content or amino acid analysis.

Reaction Conditions

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

General conditions for common peptide manipulations (literature/general):

• NHS-ester conjugation to Lys ε-amine: pH 7.5–8.5 in phosphate or bicarbonate buffer, 1–2 h at room temperature, molar excess of NHS-ester (e.g., 2–10×). Exclude competing amines (e.g., Tris). Quench with ethanolamine. Monitor by LC–MS.
• Maleimide chemistry: If a cysteine is introduced synthetically (not present in KYFIL), perform at pH 6.5–7.0 to favor thiol selectivity. Not directly applicable to this sequence without modification.
• Tyrosine-specific labeling (diazonium coupling): Mildly basic conditions (pH 8–9) with aryl diazonium salts; control stoichiometry and time to limit over-modification. Validate by MS and UV–Vis.
• Click chemistry: If an azide/alkyne handle is installed on termini or side chains, CuAAC under Cu(I) catalysis (e.g., CuSO4/sodium ascorbate, TBTA ligand) at room temperature in aqueous/tert-butanol mixtures; thoroughly remove copper post-reaction for bioassays.
• Stock solution preparation: Dissolve as described in Solvent Selection; filter if needed. For sensitive assays, prepare fresh working solutions and keep on ice. All conditions above are literature/general guidance and must be optimized empirically for the specific sequence and application.

Safety and Handling

Item-specific hazard data:

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

General laboratory safety for peptides (literature/general):

• PPE: Wear lab coat, safety glasses, and appropriate gloves (e.g., nitrile). Avoid inhalation of powders and prevent skin/eye contact. Work in a clean area; use a fume hood when weighing fine powders or when using organic co-solvents.
• Handling: Minimize aerosolization. Allow vial to equilibrate to room temperature in a desiccator before opening to reduce moisture condensation. Avoid repeated freeze–thaw of solutions; prepare single-use aliquots.
• Incompatibilities: Strong oxidizers may degrade peptides; avoid prolonged exposure to strong acids/bases unless used transiently for dissolution. Protect from light if sequence contains photosensitive residues (e.g., Tyr) to limit photo-oxidation.
• First aid (overview): If inhaled, move to fresh air; if on skin/eyes, rinse with water; if ingested, rinse mouth. Seek medical attention as per institutional SOPs. Defer to the SDS for authoritative guidance.
• Waste: Dispose of peptide solutions and contaminated materials according to institutional chemical/biological waste procedures. Storage conditions (from Product Data): Store at −20°C. Shipped in ice chest with ice pads to maintain cold chain.

Solvent Selection

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

General strategy for dissolving short, partly hydrophobic peptides (literature/general):

• Initial approach: Start with high-purity water. If insoluble, acidify slightly (e.g., add small aliquots of 0.1%–1% HCl or acetic acid) to protonate Lys and improve solubility. Gentle heating (≤37°C) and sonication can help.
• Co-solvents: For sequences with Tyr/Phe/Ile/Leu, use minimal volumes of DMSO (e.g., 5–20% v/v in final buffer) or add a small volume of DMSO to wet the powder before diluting with aqueous buffer. Alternatively, use ethanol or isopropanol in low percentages if compatible with assays.
• Buffers: After dissolution, adjust to the desired buffer (e.g., PBS, HEPES) and pH for your application. Avoid strong basic pH unless required, as it may promote side reactions (e.g., deamidation) over time.
• Salt form/counter-ions: TFA salts can lower solution pH; neutralize appropriately after dissolution when necessary.
• Filtration: Use low-protein-binding 0.22 µm filters if sterile solutions are required. Assess adsorption on plastics for hydrophobic peptides; glass vials or siliconized tubes can reduce losses. Comparison (general):
• Water/acidified water: Greenest, best first choice.
• DMSO: Powerful co-solvent; ensure assay tolerance.
• Urea/guandine HCl: Useful denaturants for difficult sequences; may disrupt biological assays.

Storage and Reconstitution

Item-specific storage (from Product Data):

• Store at −20°C.
• Shipped in ice chest with ice pads to maintain cold chain.

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

General reconstitution guidance for peptides (literature/general):

• Before opening: Allow the sealed vial to equilibrate to room temperature in a desiccator to prevent condensation. Briefly spin down to collect material.
• Solubilization: Start with water or lightly acidified water. If insoluble, add a minimal volume of DMSO to wet the peptide, then dilute with buffer. Adjust pH as needed for complete dissolution.
• Aliquoting: Prepare single-use aliquots at convenient concentrations to avoid repeated freeze–thaw cycles. Use low-binding or glass vials to reduce adsorption of hydrophobic sequences.
• Storage of solutions: Store aliquots at −20°C for short-to-medium term. For longer storage, consider −80°C. Avoid multiple freeze–thaw cycles; thaw on ice and use promptly. Protect light-sensitive conjugates (if generated) with foil.
• Stability: Sequence- and formulation-dependent. Monitor by analytical HPLC/LC–MS over time. Do not store in strong base or oxidizing environments. Always consult the CoA/Spec Sheet and SDS for lot-specific guidance and observe institutional best practices for handling and storage.

Structure and Identity

• SKU: D1442359
• Product Name: d-KYFIL
• CAS: D1442359 (catalog placeholder)
• 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.

General structural interpretation (literature/general):

• The name “d-KYFIL” suggests a short peptide comprising the amino acid one-letter codes K–Y–F–I–L, with a D-configuration at the first residue (D-Lys) unless otherwise indicated. This implies a pentapeptide with a basic side chain (Lys), an aromatic phenol (Tyr), an aromatic ring (Phe), and two hydrophobic aliphatic residues (Ile, Leu).
• Functional groups expected for an unmodified peptide include: N-terminus (free amine), internal amide bonds (peptide backbone), and a C-terminus (carboxylate or amide, depending on final protection/capping). Side-chain functionalities: ε-amine (Lys), phenolic hydroxyl (Tyr), aromatic rings (Tyr/Phe), and aliphatic side chains (Ile/Leu).
• Stereochemistry: At minimum, the “d-” prefix indicates one D-amino acid; remaining residues are typically L unless specified. Exact stereochemical pattern and any terminal capping are not specified for this item; refer to CoA/Spec Sheet.

Synthetic Utility

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

General synthetic and chemical utility of a KYFIL-type peptide (literature/general):

• Functional handles for derivatization: ε-Amine of Lys enables selective acylation, carbamylation, and conjugation via NHS-esters or isothiocyanates. Tyr’s phenolic OH can be modified (e.g., etherification/esterification under suitable conditions) or undergo diazo coupling. N-terminus and C-terminus (if free) provide additional points for functionalization (e.g., biotinylation, fluorescent labeling, carrier attachment).
• Stereochemical probe: Incorporation of a D-residue at the N-terminus is a useful tactic to probe conformation–activity relationships, protease resistance, and receptor selectivity versus the all-L sequence.
• Building block/fragment: Serves as a defined oligomer for assembling longer constructs via native chemical ligation or stepwise coupling (if termini are appropriately protected/activated; not specified for this item).
• Surface chemistry: Primary amines can anchor peptides onto activated surfaces (e.g., NHS-ester functionalized beads/slides) to create affinity materials or microarrays.
• Analytical method development: Utilize as a known mass/sequence for tuning LC–MS parameters (ionization mode, collision energies) and retention modeling in reversed-phase separations.

Target Specificity

Item-specific target/epitope/clone/isotype information: Not applicable. This product is a peptide reagent, not an antibody or affinity reagent with defined biological target specificity.

• Target specificity data: Not specified for this item; refer to CoA/Spec Sheet if any binding/assay validation is provided by the end user.
• Recommendation: If used as a ligand or probe, determine binding specificity experimentally (e.g., competition assays, SPR/ITC, or receptor-binding studies) under your assay conditions.