Ser-Phe - ≥95% , CAS No.16875-28-8

CAS: 16875-28-8 Cat. No.: S1041595 PubChem CID: 7009598

GRADE & PURITY ≥95%

Storage

Room temperature

Specifications

Spezifikationen & Reinheit

≥95%

Storage

Room temperature

Reinheit

≥95%

Namen und Kennungen

• Kanonisches Lächeln: C1=CC=C(C=C1)CC(C(=O)O)NC(=O)C(CO)N
• IUPAC Name: (2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-phenylpropanoic acid
• InChIKey: PPQRSMGDOHLTBE-UWVGGRQHSA-N
• INCHI: 1S/C12H16N2O4/c13-9(7-15)11(16)14-10(12(17)18)6-8-4-2-1-3-5-8/h1-5,9-10,15H,6-7,13H2,(H,14,16)(H,17,18)/t9-,10-/m0/s1
• Isomere SMILES: C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CO)N
• Alternative CAS-Nummer: 16875-28-8
• PubChem CID: 7009598

Taxonomic Classification

Taxonomy Tree

• Kingdom Organic compounds
  • Superclass Organic acids and derivatives
    • Klasse Carboxylic acids and derivatives
      • Subclass Amino acids, peptides, and analogues
        • Ebene5 Peptides
          • Ebene6 Dipeptides

• Kingdom: Organic compounds
• Superclass: Organic acids and derivatives
• Klasse: Carboxylic acids and derivatives
• Subclass: Amino acids, peptides, and analogues
• Intermediate Tree Nodes: Peptides
• Direct Parent: Dipeptides
• Alternative Parents: Phenylalanine and derivatives N-acyl-L-alpha-amino acids Serine and derivatives Alpha amino acid amides Phenylpropanoic acids Amphetamines and derivatives Secondary carboxylic acid amides Amino acids Carboxylic acid salts Monocarboxylic acids and derivatives Carboxylic acids Organopnictogen compounds Monoalkylamines Hydrocarbon derivatives Primary alcohols Carbonyl compounds Organic oxides Organic salts Organic zwitterions
• Molecular Framework: Aromatic homomonocyclic compounds
• Substituents: Alpha-dipeptide - Phenylalanine or derivatives - N-acyl-alpha amino acid or derivatives - N-acyl-alpha-amino acid - N-acyl-l-alpha-amino acid - Alpha-amino acid amide - Serine or derivatives - 3-phenylpropanoic-acid - Amphetamine or derivatives - Alpha-amino acid or derivatives - Monocyclic benzene moiety - Benzenoid - Amino acid - Amino acid or derivatives - Carboxamide group - Carboxylic acid salt - Secondary carboxylic acid amide - Carboxylic acid - Monocarboxylic acid or derivatives - Alcohol - Organonitrogen compound - Organooxygen compound - Primary alcohol - Primary aliphatic amine - Primary amine - Organic zwitterion - Organic salt - Carbonyl group - Hydrocarbon derivative - Organic oxide - Organopnictogen compound - Amine - Organic oxygen compound - Organic nitrogen compound - Aromatic homomonocyclic compound
• Beschreibung: This compound belongs to the class of organic compounds known as dipeptides. These are organic compounds containing a sequence of exactly two alpha-amino acids joined by a peptide bond.
• External Descriptors: dipeptide

Data sources

1. Djoumbou Feunang Y, Eisner R, Knox C, Chepelev L, Hastings J, Owen G, Fahy E, Steinbeck C, Subramanian S, Bolton E, Greiner R, and Wishart DS. ClassyFire: Automated Chemical Classification With A Comprehensive, Computable Taxonomy. Journal of Cheminformatics, 2016, 8:61.

DOI: 10.1186/s13321-016-0174-y

Chemische und physikalische Eigenschaften

• Molekulargewicht: 252.270 g/mol
• XLogP3: -3.500
• Hydrogen Bond Donor Count: 4
• Hydrogen Bond Acceptor Count: 5
• Rotatable Bond Count: 6
• Exact Mass: 252.111 Da
• Monoisotopic Mass: 252.111 Da
• Topological Polar Surface Area: 113.000 Ų
• Heavy Atom Count: 18
• Formal Charge: 0
• Complexity: 290.000
• Isotope Atom Count: 0
• Defined Atom Stereocenter Count: 2
• Undefined Atom Stereocenter Count: 0
• Defined Bond Stereocenter Count: 0
• Undefined Bond Stereocenter Count: 0
• The total count of all stereochemical bonds: 0
• Covalently-Bonded Unit Count: 1

Application Protocols

No item-specific tested application protocols are provided for this product. For general laboratory use, consider the following literature-based starting points (adjust as needed):

• Stock solutions:

  • Aqueous: dissolve at 1–100 mM in water or buffer (pH 3–8); gentle heating/sonication may assist. Filter sterilize (0.22 µm) if sterility is required.
  • Organic: prepare 100–500 mM in DMSO or DMF for subsequent dilution into aqueous media; keep final organic content ≤1–2% in bioassays.

• LC–MS reference standard preparation:

  • Dilute to 10–100 µg/mL in water/acetonitrile (1:1) with 0.1% formic acid; inject 1–5 µL; monitor at 214 and 257–260 nm and by ESI+ MS.

• Enzymatic assays (peptidase/transport in vitro):

  • Use buffered saline (e.g., 50 mM phosphate, pH 7.4) with peptide concentrations in the 10–500 µM range; quantify by HPLC/LC–MS.

These are general suggestions only; optimize conditions for your specific system. Always consult the item’s CoA/SDS for any constraints specific to this lot or form.

Biological Roles

General literature context for the Ser–Phe dipeptide (no medical or clinical claims):

• Transport and uptake: small peptides are recognized by proton-coupled oligopeptide transporters (e.g., PEPT1/PEPT2) in epithelial systems. Ser–Phe, bearing mixed polarity, is a useful model to probe such transport in vitro.
• Metabolism: dipeptidases and aminopeptidases can hydrolyze Ser–Phe to its constituent amino acids; kinetics depend on enzyme specificity and stereochemistry.
• Physicochemical behavior: the serine hydroxyl promotes hydrogen bonding and aqueous compatibility, while the phenylalanine benzyl side chain introduces hydrophobic and π–π interaction potential. This amphiphilicity influences conformational preferences and interactions with membranes, carriers, and chromatographic phases.
• Analytical relevance: aromatic absorption from phenylalanine provides convenient UV detection (∼257–260 nm, literature) and facilitates LC–MS method development with mixed-mode retention behavior.
• Structure–activity exploration: Ser–Phe is often part of peptide motif studies assessing how polar/hydrophobic juxtaposition affects binding to proteins or materials surfaces (e.g., adsorption to C18 silica or polymer supports).

Buffer Applications

This product is a dipeptide and is not typically used as a buffering agent. It lacks a defined, narrow pH range with high buffering capacity compared to standard buffers (e.g., phosphate, HEPES, Tris).

• Practical note: When working with Ser–Phe in biological assays, select an appropriate buffer system (e.g., phosphate, acetate, HEPES) based on the assay pH and ionic strength requirements. Adjust buffer pH to modulate peptide ionization state and solubility as needed.
• For specific buffer recipes and pH ranges, refer to established buffering systems rather than attempting to use Ser–Phe itself as a buffer component.

Green Alternatives

Peptide manipulations often rely on polar aprotic solvents and coupling reagents with varying EHS profiles. When working with Ser–Phe, consider greener substitutions where feasible (literature/general guidance):

• Solvents:

  • Replace DMF/NMP with safer alternatives when possible: aqueous-buffered systems, ethanol, 2-MeTHF, acetone, or propylene carbonate for certain steps.
  • For RP-HPLC, reduce acetonitrile consumption by using methanol where compatible with resolution/pressure.

• Coupling reagents and additives:

  • Favor OxymaPure with EDC or DIC as a safer alternative to HOBt/HOAt (avoid dry HOBt/HOAt due to explosivity concerns).
  • Explore enzymatic ligation (e.g., sortase, protease-mediated) or aqueous carbodiimide reactions for specific applications.

• Work-up and purification:

  • Minimize chlorinated solvents; use ethyl acetate/2-MeTHF/IPA in extractions when compatible.
  • Optimize gradient and load to reduce HPLC runs; recycle solvents where validated.

Comparison (general, illustrative):

• DMF vs aqueous buffer with cosolvent: buffer reduces toxicity and facilitates greener waste streams; may limit solubility at high concentrations.
• HATU vs EDC/Oxyma: EDC/Oxyma lowers hazard profile; may require optimization for difficult couplings.

Note: selectivity and yield remain paramount; pilot trials are recommended to confirm performance with greener conditions for this specific dipeptide.

Pharmaceutical Uses

No pharmacopoeial status or formulation role is specified for this item; refer to CoA/Spec Sheet. The following are general research/manufacturing contexts for dipeptides (no therapeutic claims):

• Reference standards: used to qualify analytical methods (HPLC/LC–MS) for peptide content, retention behavior, and UV response during process development.
• Process intermediates: fragments for convergent peptide synthesis in drug-substance development; Ser–Phe can be elongated at either terminus under standard coupling protocols.
• Excipient-like functions in development: in some formulations, short peptides may act as stabilizers or solubilizing aids for proteins through weak interactions (case-dependent; requires empirical validation). Not a claim for this specific item.
• Impurity markers: presence of specific dipeptides can serve as markers of proteolysis in stability studies of larger proteins/peptides.

Always confirm regulatory acceptability, impurity limits, and documentation requirements when considering any peptide material for GMP or regulated workflows.

Physical Properties

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

• Literature/general reference values for the free dipeptide Ser–Phe (for context only; actual item may differ by salt form, stereochemistry, or hydration):

  • Physical state: typically a white to off-white solid (literature, peptides).
  • Solubility: generally soluble in water and aqueous buffers; increased solubility in basic media due to carboxylate formation; also soluble in polar organics such as DMSO and formic acid; limited in nonpolar solvents (literature).
  • pKa values (typical peptide): terminal –COOH pKa ~2–3; terminal –NH3+ pKa ~8–9; serine side-chain OH pKa ~13 (not ionized under physiological pH) (literature).
  • LogP/LogD: overall hydrophilicity is moderated by one phenyl ring; logP expected low to moderate; experimental value not established here (literature expectation).
  • Optical rotation: depends on stereochemistry and solvent; not provided here (literature-dependent).
  • Melting/decomposition: many small peptides show broad decomposition >200 °C; specific value not established here (literature).

Quality and Grades

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

Context for peptide materials (general guidance):

• Common peptide grades: research grade (crude to >90%); “purified” or HPLC grade typically ≥95% area by analytical RP-HPLC; some applications require ≥98% and verified sequence identity by LC–MS and, optionally, HRMS.
• Counter-ions and form: free acid vs salts (e.g., TFA, acetate) can significantly affect mass, solubility, and chromatographic profile. Confirm the exact form on the CoA.
• Residual solvents and water content: peptides can retain water (hydration) or traces of acetonitrile/TFA from purification. Karl Fischer water and residual solvent testing may be reported on the CoA; if not, request as needed.
• Optical purity: for chiral peptides, enantiomeric/stereochemical integrity is typically confirmed via starting amino acid specs and synthesis records; chiral HPLC or enzymatic assays may be used when relevant.
• Impurities: typical related substances include deletion sequences, diastereomers (epimerization at activated centers), and protecting-group remnants. HPLC and MS profiling are standard QC tools.
• Practical note: for quantitative work, base calculations on the exact form (salt/hydrate) and assay purity listed on the CoA to prepare accurate stock solutions.

Reaction and Applications

This product is a dipeptide building block useful in peptide chemistry and analytical workflows.

• Typical research uses (literature/general):

  • Model substrate for peptide transporters (PEPT1/PEPT2) and peptidases in vitro (no clinical claims).
  • Calibration/retention-time standard in peptide LC–MS or method development due to mixed polarity (polar backbone + aromatic side chain).
  • Intermediate for elongation to longer peptides (N-terminal free amine) or fragment condensation (C-terminal carboxylate).
  • Reference compound for studying side-chain participation of serine OH in H-bonding and conformational preferences.

• Representative transformations (peptide context):

  • N-terminal acylation or labeling (e.g., NHS esters, activated carbonates) to generate amide conjugates.
  • C-terminal coupling to amines via carbodiimide (EDC/HOBt or EDC/Oxyma) or uronium reagents (HATU/HBTU) to extend sequence.
  • Protection strategies: transient protection of serine OH (e.g., TBDMS, benzyl) if required for selective modifications; typically unprotected OH is tolerated in amide couplings.

• Practical notes:

  • Control epimerization at the C-terminus of Ser–Phe during activation; use Oxyma or HOAt analogs, low temperature, and brief activation times.
  • Monitor reactions by analytical RP-HPLC and LC–MS; the aromatic Phe side chain provides UV sensitivity at 254–280 nm.
  • For aqueous bioconjugations, employ water-miscible solvents (DMF/DMSO) at low percentages and maintain pH appropriate for amine nucleophilicity (pH 7.5–8.5).

Reaction Conditions

General literature conditions for manipulating Ser–Phe in solution-phase peptide chemistry (not item-specific):

• Amide coupling (C-terminus of Ser–Phe to an amine):

  • Reagents: EDC·HCl (1.1–1.5 eq) + OxymaPure (1.1–1.5 eq) and DIPEA (2–3 eq) in DMF or DMF/DCM at 0–25 °C; reaction 1–4 h. Alternative: HATU (1.05–1.2 eq) + DIPEA.
  • Tips: pre-cool and minimize pre-activation time to limit epimerization; monitor by RP-HPLC.

• N-terminal acylation (forming an amide at N-terminus):

  • Reagents: acid chlorides or NHS esters (1.1–1.5 eq) in aqueous-organic media (buffered pH 8–9) or DMF with base; 0–25 °C, 0.5–2 h.
  • Aqueous option: EDC coupling to carboxylic acids in MES buffer (pH ~5.5–6.0) with NHS/Oxyma.

• Side-chain modifications (serine OH):

  • Carbonate formation: p-nitrophenyl chloroformate (1.1 eq) in dry DCM/DMF, 0 °C to rt, with base; subsequent amine capture forms carbamates.
  • Protection (if required): TBDMS-Cl or benzyl protection under standard conditions; ensure compatibility with peptide backbone and planned deprotection sequence.

• Purification:

  • RP-HPLC with water/acetonitrile + 0.1% formic or TFA; gradients 5–60% over 15–30 min; detect at 214 nm (peptide bond) and 254–280 nm (Phe).

• Typical outcomes:

  • Clean couplings often reach >80–90% conversion within 1–3 h under optimized conditions (literature); isolate as lyophilized solid after preparative HPLC.

Safety and Handling

• Item-specific hazard information: Not specified for this item; refer to CoA/Spec Sheet and SDS.
• GHS classification, signal word, H-statements, pictograms: Not specified for this item; refer to SDS.

General laboratory guidance for small peptides (literature/best practice):

• PPE: laboratory coat, safety glasses, and appropriate gloves (e.g., nitrile). Avoid inhalation of dust/aerosols; handle powders in a ventilated enclosure if possible.
• Incompatibilities: strong oxidizers may react with the aromatic ring or peptide backbone under forcing conditions; avoid strong acids/bases for prolonged periods if preserving sequence integrity is critical.
• Hygroscopicity: many peptides can be mildly hygroscopic; keep container tightly closed to prevent moisture uptake and caking.
• First aid overview: if inhaled, move to fresh air; if on skin or in eyes, rinse with water; if ingested, rinse mouth. Seek medical attention if symptoms persist. Always follow SDS for authoritative guidance.
• Thermal stability: peptides may darken or decompose on strong heating; avoid excessive temperatures during drying.
• Dust control: minimize dust generation; clean spills with damp disposable towels or HEPA-filtered vacuum to avoid aerosolization.
• Waste: dispose according to institutional and local regulations for organic laboratory chemicals.

Solvent Selection

Ser–Phe is a small, amphiphilic dipeptide with a polar backbone/serine OH and one hydrophobic aromatic side chain.

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

Literature-based solvent guidance:

• Primary choices: water or aqueous buffers (pH 2–8) often provide good solubility; gentle warming and sonication may help dissolution. Adjusting pH above the carboxylate pKa increases solubility via deprotonation.
• Organic cosolvents: DMSO, DMF, and methanol are effective for stock solutions; for LC–MS, water/acetonitrile with 0.1% formic acid is common.
• Avoid: nonpolar solvents (hexanes, toluene) where peptide solubility is typically negligible.

Comparison (literature, general):

• Water/buffer: best for bioassays and enzymology; pH control prevents aggregation/ionization artifacts.
• DMSO: maximizes concentration for hydrophobic sequences; dilute into buffer immediately before use to ≤1–2% v/v in assays.
• MeOH/EtOH: moderate solubility, useful for analytical sample prep; may impact some bioassays.
• Formic or acetic acid (0.1–1%): improves peak shape in LC–MS and protonates amines; use volatile acids if MS detection is needed.

Practical tips:

• Filter through 0.22 µm for analytical injections.
• For poorly soluble lots, prepare a small DMSO concentrate (e.g., 50–100 mM) then dilute into buffered aqueous media with mixing to the desired working concentration.

Storage and Reconstitution

• Item-specific storage: Room temperature (as provided). For best practice, store tightly closed, in a dry place, away from direct light. If long-term storage is anticipated, many users prefer 2–8 °C to limit hydrolysis and moisture uptake; confirm acceptability with the CoA.
• Shipped in: Not specified for this item; refer to CoA/Spec Sheet.

Reconstitution and handling (general guidance for dipeptides):

• Solvents: water or buffer (pH 3–8) are preferred; DMSO or DMF can be used to prepare concentrated stocks for later dilution.
• Concentration: prepare aliquots at working concentrations to avoid repeated freeze–thaw. If frozen stocks are made, store at −20 °C and thaw on ice; avoid more than 3–4 freeze–thaw cycles.
• Filtration: for sterile applications, 0.22 µm PVDF or PES filtration after dissolution.
• Stability: aqueous solutions are generally stable for hours to days at 2–8 °C; for longer storage, freeze aliquots. Avoid prolonged exposure to strong acids/bases or elevated temperatures.
• Documentation: verify exact salt form, hydration state, and assay purity on the CoA to calculate accurate molar concentrations upon reconstitution.

Structure and Identity

Ser-Phe is the dipeptide composed of serine and phenylalanine (sequence Ser–Phe).

• Item-specific (from Product Data):

  • Product name: Ser-Phe
  • CAS: 16875-28-8
  • InChIKey: 283780 (as provided)
  • SMILES: 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.

• Literature/typical structural information (for the free dipeptide, Ser–Phe, free N-terminus and C-terminal carboxylic acid; provided for reference only):

  • Common 2D features: an N-terminal α-amino group, a central peptide amide bond, and a C-terminal carboxylic acid; serine side chain bears a primary alcohol (–CH2–OH); phenylalanine side chain is benzyl (–CH2–C6H5).
  • Possible stereochemistry: four stereochemical variants exist (L/L, L/D, D/L, D/D) at the two α-carbons; typical biological form is L-Ser–L-Phe.
  • Example literature SMILES (L-Ser–L-Phe, free acid): NC@@HC(=O)NC@@HC(=O)O
  • Example literature InChIKey (L-Ser–L-Phe, free acid): not provided here; consult reference databases.
  • Example empirical formula and formula mass (free dipeptide): C12H16N2O4; Mr ≈ 252.27 g/mol (literature).

• Structural description in words: a linear dipeptide where the serine carboxyl group is condensed with the α-amino of phenylalanine, forming an amide (peptide) linkage; polar termini flank one polar side chain (serine OH) and one hydrophobic aromatic side chain (phenylalanine).

Synthetic Utility

As a bifunctional building block, Ser–Phe offers both an N-terminal amine and a C-terminal carboxylate for peptide assembly and derivatization.

• Functional handles:

  • N-terminus: nucleophilic amine for acylation, urea/carbamate formation, isothiocyanate/activated ester labeling.
  • C-terminus: activation to mixed anhydrides, NHS esters, or uronium-mediated active species for amide bond formation with amines.
  • Serine side chain: primary alcohol for esterification, carbonate formation, or selective oxidation (e.g., to aldehyde via periodate after suitable protection strategies in larger peptides; handle with care to avoid backbone damage).
  • Phenylalanine side chain: aromatic substitution not typically reactive, but enables π-stacking interactions in affinity/materials applications.

• Retrosynthetic use:

  • Fragment coupling in convergent peptide synthesis: Ser–Phe can serve as a dipeptidyl donor/acceptor with minimal protecting-group complexity if termini are appropriately protected during multistep assembly.

• Analytical leverage:

  • UV chromophore from Phe (∼257–260 nm, literature) aids HPLC monitoring; MS ionization robust under ESI+.

• Selectivity notes:

  • Manage potential epimerization during C-terminal activation; employ Oxyma-based protocols, low temperature, and rapid couplings to preserve stereochemical integrity (if chiral form is relevant).

Target Specificity

Not applicable to this product type. Ser–Phe is a small-molecule/dipeptide, not an antibody, protein, or nucleic acid probe. No antigen/epitope, clone, isotype, or species reactivity data are relevant.