Glu-Ser - ≥97% , CAS No.5875-38-7

CAS: 5875-38-7 Cat. No.: G1041593 PubChem CID: 6995653

GRADE & PURITY ≥97%

Storage

Room temperature

Specifications

Especificações e pureza

≥97%

Condições de armazenamento de armazenamento

Room temperature

Pureza

≥97%

Nomes e identificadores

• Sorrisos canónicos: C(CC(=O)O)C(C(=O)NC(CO)C(=O)O)N
• IUPAC Name: (4S)-4-amino-5-[[(1S)-1-carboxy-2-hydroxyethyl]amino]-5-oxopentanoic acid
• InChIKey: UQHGAYSULGRWRG-WHFBIAKZSA-N
• INCHI: 1S/C8H14N2O6/c9-4(1-2-6(12)13)7(14)10-5(3-11)8(15)16/h4-5,11H,1-3,9H2,(H,10,14)(H,12,13)(H,15,16)/t4-,5-/m0/s1
• SMILES isoméricas: C(CC(=O)O)[C@@H](C(=O)N[C@@H](CO)C(=O)O)N
• CAS alternativo: 5875-38-7
• PubChem CID: 6995653

Taxonomic Classification

Taxonomy Tree

• Kingdom Organic compounds
  • Superclass Organic acids and derivatives
    • Classe Carboxylic acids and derivatives
      • Subclass Amino acids, peptides, and analogues
        • Level5 Peptides
          • Level6 Dipeptides

• Kingdom: Organic compounds
• Superclass: Organic acids and derivatives
• Classe: Carboxylic acids and derivatives
• Subclass: Amino acids, peptides, and analogues
• Intermediate Tree Nodes: Peptides
• Direct Parent: Dipeptides
• Alternative Parents: Glutamic acid and derivatives N-acyl-L-alpha-amino acids Serine and derivatives Alpha amino acid amides Amino fatty acids Beta hydroxy acids and derivatives Hydroxy fatty acids N-acyl amines Dicarboxylic acids and derivatives Secondary carboxylic acid amides Amino acids Carboxylic acids Hydrocarbon derivatives Carbonyl compounds Monoalkylamines Organic oxides Organopnictogen compounds Primary alcohols
• Molecular Framework: Aliphatic acyclic compounds
• Substituents: Alpha-dipeptide - Glutamic acid 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 - Alpha-amino acid or derivatives - Amino fatty acid - Beta-hydroxy acid - Hydroxy fatty acid - Fatty acid - Hydroxy acid - Fatty acyl - N-acyl-amine - Fatty amide - Dicarboxylic acid or derivatives - Amino acid or derivatives - Carboxamide group - Amino acid - Secondary carboxylic acid amide - Carboxylic acid - Primary amine - Organic oxygen compound - Hydrocarbon derivative - Organic nitrogen compound - Carbonyl group - Organic oxide - Organopnictogen compound - Alcohol - Amine - Primary aliphatic amine - Primary alcohol - Organooxygen compound - Organonitrogen compound - Aliphatic acyclic compound
• Descrição: 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

Propriedades químicas e físicas

• Peso molecular: 234.210 g/mol
• XLogP3: -4.800
• Hydrogen Bond Donor Count: 5
• Hydrogen Bond Acceptor Count: 7
• Rotatable Bond Count: 7
• Exact Mass: 234.085 Da
• Monoisotopic Mass: 234.085 Da
• Topological Polar Surface Area: 150.000 Ų
• Heavy Atom Count: 16
• Formal Charge: 0
• Complexity: 280.000
• 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 tested application protocols are provided for this item. General starting points for common research uses (literature-based suggestions; optimize empirically):

• LC–MS reference solution:

  • Dissolve accurately weighed Glu-Ser in LC–MS grade water to prepare a 1–10 mM stock. Filter (0.22 µm) if particulate is observed. Dilute to working levels (1–100 µM) in starting mobile phase.

• Enzymatic assay substrate:

  • Prepare a fresh aqueous stock (e.g., 10–50 mM) in assay buffer (pH ~7–8). Keep on ice during use and avoid repeated freeze–thaw of aliquots. Monitor hydrolysis by HPLC or colorimetric coupled assays.

• Coupling reagent test reaction:

  • Combine Glu-Ser (1.0 eq) with an amine partner (1.1 eq) and EDC (1.2 eq) plus NHS (1.2 eq) in MES buffer pH 5.5 at 0–25 °C. Quench and analyze conversion by LC.

These are generic literature-style examples; they are not validated protocols for SKU G1041593. For item-specific recommendations, consult the CoA/Spec Sheet.

Biological Roles

This product is intended for research use only. The following describes general, literature-based roles of Glu–Ser motifs and small dipeptides in biochemistry; it is not a statement of physiological or clinical function for this specific item.

• Transport and metabolism (literature):

  • Small dipeptides can be taken up by peptide transporters (e.g., PEPT family in various organisms) and hydrolyzed by dipeptidases, providing a tractable system to study peptide handling and hydrolysis kinetics.

• Structural/biophysical context:

  • The Glu side-chain carboxylate contributes negative charge and metal-binding potential; the Ser hydroxyl is a hydrogen-bond donor/acceptor, influencing local secondary structure preferences and interaction with solvents.

• Enzymology probes:

  • Glu-Ser sequences can be used as minimal substrates or competitive probes to examine specificity in enzymes recognizing acidic–polar pairs at P1–P2 positions (notation varies by enzyme; literature context).

• Analytical standards:

  • Dipeptides serve as mass spec and chromatography references to benchmark retention behavior as a function of polarity and charge state.

No therapeutic or clinical claims are made or implied. Verify stereochemistry and salt/form on the CoA if biological recognition specificity is relevant to your experiments.

Buffer Applications

Glu-Ser is not a conventional buffering agent and is not typically used to formulate buffer systems with defined pH ranges. Its acid/base groups can contribute to solution buffering capacity over limited ranges, but for reproducible buffering one should select established buffers (e.g., phosphate, HEPES, MOPS).

• Practical guidance:
  • If preparing aqueous solutions of Glu-Ser for assays, dissolve in an appropriate pre-made buffer (e.g., 10–50 mM phosphate, pH 7.0–7.4; or HEPES, pH 7.2–7.8) to maintain stable pH.
  • Avoid relying on the dipeptide alone to control pH, as its titration profile and ionic strength effects are not standardized for buffering applications.

For buffer formulations, consult established buffer tables and use Glu-Ser as a solute or analyte within those systems rather than as the buffering component.

Green Alternatives

For aqueous-compatible dipeptides like Glu-Ser, greener practice focuses on maximizing water use, minimizing hazardous organic solvents, and selecting low-toxicity reagents in any coupling or analytical procedure.

• Prefer aqueous media:

  • Use water or buffered aqueous solutions as primary solvents for dissolution, storage, and assays when feasible. This reduces VOC emissions and waste.

• Greener cosolvents (literature perspective):

  • Replace high-toxicity aprotics (e.g., DMF, NMP) with water/DMSO blends at low DMSO %, ethanol, or glycerol where method-compatible.

• Peptide coupling (if extending sequences, literature guidance):

  • Consider water-compatible coupling systems (e.g., EDC·HCl with NHS or HOAt alternatives such as ethyl cyano(hydroxyimino)acetate) under buffered conditions to avoid chlorinated solvents.
  • Use catalytic green bases (e.g., bicarbonate) in water or 2-MeTHF when solution-phase coupling is required.

• Waste minimization:

  • Prepare concentrated stocks and dilute at point-of-use to reduce container and solvent waste.
  • Adopt microscale assays and LC methods with shorter gradients and aqueous-rich mobile phases when resolution permits.

Comparison (general):

• Water/buffer: lowest environmental impact; may need pH control for solubility.
• Ethanol: renewable, low toxicity; limited solvency vs DMSO.
• DMSO: good solvency at low amounts; higher aquatic persistence than ethanol—use sparingly.

Pharmaceutical Uses

No pharmacopeial status, excipient role, or formulation specifications are provided for this item. This product is supplied for research use only.

• General laboratory/CMC-adjacent uses (literature/good practice, non-clinical):
  • Reference standard in analytical methods (e.g., LC–MS system suitability for small peptides).
  • Process development studies exploring peptide stability, degradation pathways (hydrolysis, racemization), and adsorption losses on contact materials.
  • Excipient-like roles are uncommon for unmodified dipeptides such as Glu-Ser; if a peptide-based functional excipient is needed, materials with documented regulatory monographs should be considered.

Any use in manufacturing or clinical settings requires independent suitability assessment and is outside the scope of this research-use-only product.

Physical Properties

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

• Literature/general expectations for small, polar dipeptides (for context only):

  • State: typically a white to off-white solid (literature; item-specific appearance not provided).
  • Melting behavior: many dipeptides decompose or melt with decomposition >150 °C (literature; highly system- and stereochemistry-dependent).
  • Solubility: generally high aqueous solubility; sparingly soluble in most nonpolar organic solvents (literature). Often soluble in water, dilute buffers, and polar protic solvents such as methanol; poor solubility in hydrocarbons and ethers.
  • pKa values (qualitative): dipeptides typically show two to three titratable groups (α-NH3+/NH2, C-terminal CO2H/CO2−, plus Glu side-chain CO2H/CO2−); expect acidic pKa ~2–4 for CO2H groups and basic pKa ~8–10 for α-NH3+ (literature, ranges only).
  • LogP: strongly negative (highly hydrophilic), favoring aqueous phase (literature trend for dipeptides with acidic side chains and hydroxyl groups).
  • Optical activity: if composed of L-amino acids, solutions are optically active; absolute [α]D depends on sequence and solvent (literature).

Notes:

• Do not treat the above as specification limits. For precise values applicable to SKU G1041593, consult the product CoA/Spec Sheet and SDS.

Quality and Grades

• Grade/Purity (Product Data): Not specified for this item; refer to CoA/Spec Sheet.

• Interpreting peptide quality (general guidance):

  • Dipeptide materials are commonly qualified by purity (HPLC area %), identity (HRMS/ESI-MS, NMR), and content/water (Karl Fischer) where relevant. Impurities can include deletion sequences, residual protecting groups, and inorganic salts.
  • If intended for bioassay or analytical reference use, higher-purity material (e.g., ≥95% HPLC area) minimizes background and quantitation bias. If used as a building block for coupling, slightly lower assay purity may be acceptable but should be accounted for in stoichiometry.
  • Counterion content: free acid vs salt forms (e.g., trifluoroacetate) can affect mass balance and solubility. Confirm the counterion on the CoA.
  • Optical purity: when stereochemistry is specified (e.g., L-Glu–L-Ser), enantiopurity is typically assessed via chiral HPLC or optical rotation. This listing does not specify stereochemistry; verify on the CoA if critical to your application.

• Stabilizers/additives: Not specified for this item; refer to CoA/Spec Sheet.

• UV cutoff/trace metals/peroxide/water content: Not specified for this item; refer to CoA/Spec Sheet.

Reaction and Applications

As a dipeptide building block, Glu-Ser is useful in peptide chemistry, enzymology, and analytical method development.

• Applications (general, literature-based):

  • Enzyme substrates/standards: can serve as a minimal motif for studying peptidases (exopeptidases and dipeptidases) and peptide transporters in model systems.
  • Reference standard: calibration or retention marker for LC/MS or HPLC method development for peptides and amino acids.
  • Building block: incorporated into longer sequences by solution-phase or solid-phase peptide synthesis (SPPS) via coupling at N- or C-terminus.
  • Model compound: investigating side-chain reactivity (Glu carboxylate) and hydrogen bonding contributions from serine hydroxyl in peptide microenvironments.

• Practical notes:

  • Handling: minimize moisture uptake for accurate weighing; if hygroscopic, dry under vacuum at ambient temperature before preparing standards (refer to CoA for water content).
  • pH sensitivity: prolonged exposure to strong acid/base may lead to hydrolysis of the peptide bond; for stability during assays, maintain near-neutral pH.
  • Metal coordination: carboxylates can weakly coordinate metal ions; use metal-free buffers if metal-catalyzed side reactions are a concern in mechanistic studies.

• Related chemistry contexts:

  • Protection strategies (literature): when using as a coupling partner in synthesis, side-chain protecting groups (e.g., for Glu carboxylate) are typically used; this catalog entry does not specify protected forms, so treat as unprotected unless otherwise indicated on the CoA.

Reaction Conditions

General conditions for using Glu-Ser in coupling or derivatization reactions (literature guidance; adjust to your system):

• Solution-phase amidation to extend C-terminus:

  • Solvent: water/MeCN or water/DMF mixtures; fully aqueous possible with water-soluble coupling reagents.
  • Activation: EDC·HCl (1.1–1.5 eq) with Oxyma or NHS (1.1–1.5 eq) at pH 5.0–6.0 to limit epimerization; reaction 0–25 °C, 0.5–4 h.
  • Base control: maintain mildly acidic to neutral pH with MES or phosphate buffers; avoid strong base that promotes O→N acyl shift for serine.

• N-terminal acylation or extension:

  • Use preactivated esters (e.g., NHS esters) or carbodiimide coupling at pH 7.5–8.5; monitor by LC.

• Protecting-group considerations:

  • If side-chain selectivity is required, protect Glu side-chain carboxyl (e.g., as benzyl/tBu ester in nonaqueous chemistry) and/or serine hydroxyl. For aqueous couplings, chemoselectivity can be managed by pH and reagent choice.

• Analytical monitoring:

  • LC–MS (ESI+) readily detects protonated molecules; reversed-phase HPLC with aqueous-rich gradients (0.1% FA or acetate) provides good separation.

• Typical outcomes:

  • Small-fragment couplings often reach >70–90% conversion within hours under optimized conditions (literature); isolate as lyophilized solids after desalting.

These conditions are general literature guidance and not specifications for SKU G1041593.

Safety and Handling

• GHS/Classification (Product Data):

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

• General safety guidance for peptide solids (literature/good practice):

  • Avoid inhalation of dusts and contact with eyes/skin. Use in a well-ventilated area or fume hood when weighing dry powders.
  • Recommended PPE: lab coat, safety glasses, and appropriate chemical-resistant gloves (e.g., nitrile). Use dust mask/respirator if airborne dust may form.
  • Hygroscopicity: many dipeptides are hygroscopic; keep container tightly closed and protected from moisture to maintain mass accuracy and quality.
  • Incompatibilities: strong oxidizers may react with organic materials; avoid mixing with strong bases/acids without proper control, as hydrolysis of the peptide bond can occur under harsh conditions.

• First aid overview (always defer to SDS):

  • Inhalation: move to fresh air; seek medical attention if symptoms persist.
  • Skin/eye contact: rinse with water for several minutes; remove contaminated clothing; obtain medical advice if irritation develops.
  • Ingestion: rinse mouth; seek medical attention if unwell.

• Waste: dispose according to institutional and local regulations for nonhazardous organic laboratory chemicals unless SDS indicates otherwise.

Solvent Selection

Glu-Ser is a small, highly polar dipeptide bearing acidic and hydroxyl functionalities. Solubility behavior is governed by ionization state.

• Polarity class: strongly hydrophilic; favored in aqueous media (literature, general for dipeptides with acidic side chains).
• Aqueous systems:
  • Best solubility typically achieved in water or buffered aqueous solutions near neutral to slightly basic pH, where the Glu side chain and C-terminus are deprotonated and the α-amine may be protonated/deprotonated depending on pH.
  • For stock solutions, common choices include water, PBS, or 10–50 mM HEPES at pH 7.2–7.8 (literature practice).
• Organic cosolvents:
  • If needed for mixed systems, polar protic (MeOH, EtOH) or highly polar aprotic solvents (DMSO) can assist dissolution before dilution into water. Avoid high percentages of nonpolar solvents, which can precipitate the peptide.
• When to choose alternatives:
  • If the application requires strictly nonaqueous media, consider protected derivatives or coupling strategies that increase organic solubility (e.g., use of base and polar aprotic solvents, or temporary protecting groups).

Small comparison (literature trends):

• Water/buffer: highest biocompatibility and solubility; pH control required.
• DMSO: excellent solvating power; may interact with certain assays—keep final DMSO ≤1–2% v/v if used in bioassays.
• MeOH/EtOH: moderate aid to dissolution but can denature proteins if present during biological testing.

Storage and Reconstitution

• Storage (Product Data): Room temperature.

• Shipped In: Not specified for this item; refer to CoA/Spec Sheet.

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

• General guidance for peptide solids (good practice):

  • Keep tightly sealed in a dry, inert atmosphere (desiccator with desiccant) and protect from prolonged exposure to ambient humidity.
  • If long-term storage is planned, room temperature is acceptable per Product Data; for maximum stability, many users store peptides desiccated and protected from light. Avoid high heat.

• Reconstitution (general suggestions):

  • Use high-purity water or appropriate buffer (e.g., phosphate or HEPES, pH ~7.0–7.5). If solubility is limited initially, wet with a minimal volume of DMSO or ethanol, then dilute with water/buffer.
  • Filter sterilize (0.22 µm) if sterility is required for your application.
  • Prepare single-use aliquots to avoid repeated freeze–thaw. If freezing aliquots, store at −20 to −80 °C; thaw at room temperature before use. Note: these are general practices and not mandatory specifications for this SKU.

• Stability in solution:

  • Use freshly prepared solutions when possible. Minimize exposure to strong acid/base to avoid hydrolysis. For multi-day studies, keep solutions refrigerated and check by HPLC for degradation.

For definitive item-specific stability and reconstitution instructions, consult the CoA/Spec Sheet.

Structure and Identity

Glu-Ser is a dipeptide composed of glutamic acid and serine joined by a peptide (amide) bond. Without stereochemical qualifiers in the listing, the exact configuration (e.g., L-Glu–L-Ser vs other isomers) is not specified.

• Product Data identifiers (as provided):

  • CAS: 5875-38-7
  • InChIKey: 366497 (as provided in Product Data)
  • 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/computed descriptors (general for Glu–Ser dipeptides; stereochemistry not specified here):

  • Typical sum formula for a Glu–Ser dipeptide (any linkage) after peptide bond formation: approximately C8H14N2O6 (literature/computed).
  • Approximate formula weight: ~234.2 g/mol (literature/computed).

• Structural features (general):

  • One backbone amide (peptide) bond linking the α-carboxyl of glutamic acid to the α-amino of serine (for the common α–α linkage).
  • Side chains: glutamate bears a γ-carboxylate functionality; serine bears a primary alcohol (–CH2OH).
  • Functional group inventory: secondary amide, carboxylic acid (or carboxylate depending on pH), primary alcohol, α-amino (protonation state pH-dependent).
  • 2D description in words: An N-terminal amino acid residue with a free α-amino (pH-dependent) attached to –CH(CONH–)–CO–, linked via –CONH– to the serine α-carbon bearing –CH2OH, terminating at a C-terminal carboxyl (pH-dependent). If Glu is N-terminal, the Glu side chain extends as –CH2–CH2–CO2H.

Synthetic Utility

Glu-Ser serves as a useful fragment in peptide synthesis and as a model substrate in solution-phase reactions.

• Functional group handles:

  • N-terminus (α-amine, protonation state pH-dependent) for acylation/coupling to extend peptides at the N-end.
  • C-terminus (carboxylic acid) for activation and coupling to amines (amide formation) to extend at the C-end.
  • Glutamate side-chain carboxylate can participate in coupling if side-chain protection is absent; control with protecting groups to avoid branching.
  • Serine hydroxyl can be transiently protected (e.g., as tBu, benzyl, or TBDMS in nonaqueous routes) to prevent side reactions such as O-acylation.

• Named methods and strategies (literature):

  • Carbodiimide-mediated couplings (EDC/HOBt or EDC/Oxyma) in aqueous or mixed solvents.
  • Active ester routes (NHS esters) for mild amide formation.
  • SPPS compatibility as a preformed dipeptide unit when orthogonal protection patterns are appropriate.
  • Enzymatic ligation/peptidase-catalyzed synthesis in buffered aqueous media for greener transformations.

• Retrosynthetic value:

  • Can simplify assembly of sequences containing Glu–Ser motifs by convergent fragment coupling, potentially improving overall yields and reducing epimerization events when handled under mild conditions.

Target Specificity

Not applicable. This product is a small-molecule/dipeptide standard and is not an antibody or affinity reagent. No antigen, epitope, clone, isotype, or species reactivity is associated with this item.