DL-β-Homoleucine - ≥98% , CAS No.3653-34-7

CAS: 3653-34-7 Cat. No.: D404546 Formula: C₇H₁₅NO₂ Peso molecolare: 145.2 Numero EC: 625-658-1

GRADE & PURITY ≥98%

Synonyms

FT-0630327 | AKOS005071399 | DL-.beta.-Homoleucine | STK504558 | BB 0260066 | DL-beta-Homoleucine, >=99.0% (NT) | DL-beta-Homoleucine | SCHEMBL2377939 | (+-)-3-amino-5-methyl-hexanoic acid | 8T-0019 | J-800387 | SY058864 | 3-Amino-5-methylhexanoicacid | E

Storage

Room temperature

Specifications

Sinonimi

FT-0630327 | AKOS005071399 | DL-.beta.-Homoleucine | STK504558 | BB 0260066 | DL-beta-Homoleucine, >=99.0% (NT) | DL-beta-Homoleucine | SCHEMBL2377939 | (+-)-3-amino-5-methyl-hexanoic acid | 8T-0019 | J-800387 | SY058864 | 3-Amino-5-methylhexanoicacid | E

Specifiche e purezza

≥98%

Condizioni di conservazione di stoccaggio

Room temperature

Purezza

≥98%

Nomi e identificatori

Pubchem Sid

488192430

Pubchem Sid Url

https://pubchem.ncbi.nlm.nih.gov/substance/488192430

Sorrisi canonici

CC(C)CC(CC(=O)O)N

IUPAC Name

3-amino-5-methylhexanoic acid

InChIKey

MLYMSIKVLAPCAK-UHFFFAOYSA-N

INCHI

1S/C7H15NO2/c1-5(2)3-6(8)4-7(9)10/h5-6H,3-4,8H2,1-2H3,(H,9,10)

Isomeri SMILES

CC(C)CC(CC(=O)O)N

Peso molecolare

145.2

Reaxy-Rn

1722065

Reaxys-RN_link_address

https://www.reaxys.com/reaxys/secured/hopinto.do?context=S&query=IDE.XRN=1722065&ln=

Taxonomic Classification

Taxonomy Tree

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

• Kingdom: Organic compounds
• Superclass: Organic acids and derivatives
• Classe: Carboxylic acids and derivatives
• Subclass: Amino acids, peptides, and analogues
• Intermediate Tree Nodes: Amino acids and derivatives
• Direct Parent: Beta amino acids and derivatives
• Alternative Parents: Medium-chain fatty acids Branched fatty acids Amino fatty acids Amino acids Monocarboxylic acids and derivatives Carboxylic acids Organopnictogen compounds Organic oxides Monoalkylamines Hydrocarbon derivatives Carbonyl compounds
• Molecular Framework: Aliphatic acyclic compounds
• Substituents: Beta amino acid or derivatives - Medium-chain fatty acid - Amino fatty acid - Branched fatty acid - Fatty acyl - Fatty acid - Amino acid - Carboxylic acid - Monocarboxylic acid or derivatives - Amine - Primary amine - Organooxygen compound - Organonitrogen compound - Hydrocarbon derivative - Primary aliphatic amine - Organic oxide - Carbonyl group - Organopnictogen compound - Organic oxygen compound - Organic nitrogen compound - Aliphatic acyclic compound
• Descrizione: This compound belongs to the class of organic compounds known as beta amino acids and derivatives. These are amino acids having a (-NH2) group attached to the beta carbon atom.
• External Descriptors: Not available

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

Proprietà chimiche e fisiche

• Punto di fusione (°C): 219 °C(dec.)
• Peso molecolare: 145.200 g/mol
• XLogP3: -1.700
• Hydrogen Bond Donor Count: 2
• Hydrogen Bond Acceptor Count: 3
• Rotatable Bond Count: 4
• Exact Mass: 145.11 Da
• Monoisotopic Mass: 145.11 Da
• Topological Polar Surface Area: 63.300 Ų
• Heavy Atom Count: 10
• Formal Charge: 0
• Complexity: 112.000
• Isotope Atom Count: 0
• Defined Atom Stereocenter Count: 0
• Undefined Atom Stereocenter Count: 1
• 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 biological assay protocols are specified for this product. As a synthetic building block, example research workflows (literature/general) include:

• Preparation of stock solutions: Dissolve in water adjusted to pH 2–3 (HCl) or pH 9–10 (NaOH), or in DMSO/DMF with a small amount of base. Filter (0.22 µm) if sterile solutions are required.
• Peptide coupling (solution): Combine protected DL-β-homoleucine (1.0 equiv), HATU (1.2 equiv), DIPEA (3 equiv) in DMF, add amine partner (1.1 equiv), stir 1–4 h at rt; monitor by LC–MS. Work up by aqueous quench and extract or precipitate as appropriate. (General guidance only.)
• SPPS incorporation: After Fmoc deprotection, couple Fmoc-β-homoleucine with HBTU/DIPEA in DMF for 2×30 min cycles to ensure complete coupling; wash and proceed with synthesis. Optimize for your sequence.

Note: These are example procedures derived from general literature practices and must be adapted/validated for specific applications. Always consult primary sources and perform small-scale trials.

Biological Roles

DL-β-Homoleucine is a non-proteinogenic β-amino acid; it is not incorporated into ribosomally synthesized proteins. The following are general, literature-based considerations for β-amino acids and leucine analogues:

• Proteolytic stability: Incorporation of β-residues into peptides often increases resistance to proteases due to altered backbone geometry and hydrogen-bonding patterns (literature/general).
• Conformational effects: β-residues can bias peptides toward distinct secondary structures (e.g., 14-helix), enabling foldamer design with tailored receptor interactions (literature/general).
• Hydrophobicity: A leucine-like, branched alkyl side chain enhances hydrophobic packing and membrane interaction propensity in designed sequences (literature/general).
• Metabolism: Free β-amino acids are typically not substrates for canonical transaminases/aminotransferases; metabolic handling differs from α-amino acids and is species- and structure-dependent (literature/general).

Note: Any biological testing must be conducted under research-use-only conditions. This product is not intended for diagnostic or therapeutic use.

Buffer Applications

DL-β-Homoleucine is not a standard biochemical buffer. However, like other amino acids, it can exhibit limited buffering capacity around its pKa values (general literature):

• Practical note: For routine buffering, dedicated systems (e.g., phosphate, Tris, HEPES, MOPS) are preferred due to defined pKa and minimal side reactions.
• Use as additive: Amino acids are sometimes used as co-solutes/osmolytes or to modulate ionic strength and solvation in protein studies. DL-β-homoleucine’s hydrophobic side chain makes it less common for such roles than glycine or alanine.
• If used: Prepare solutions in water and adjust pH with HCl/NaOH to target ranges near the amine/carboxyl pKa. Confirm solubility and absence of precipitation at working ionic strength.

For reproducible buffer performance, choose established buffering agents rather than this compound.

Green Alternatives

For synthetic workflows using DL-β-homoleucine, greener choices largely concern solvent and reagent selection rather than the building block itself.

Greener choices (literature/general):

• Solvents: Prefer water, ethanol, or 2-MeTHF over DMF/NMP when compatible. For amide couplings, use EtOAc/MeCN with water-soluble coupling systems or enzymatic catalysis.
• Coupling reagents: Consider DMTMM (less hazardous waste) or EDC with Oxyma over uronium salts to reduce HFIP/HOBt-related risks. Carbodiimide couplings in aqueous media can be effective for small molecules.
• Workup/purification: Employ aqueous crystallization/salt-switching to minimize chromatographic solvent use; use reverse-phase methods with greener eluents (water/EtOH) where possible.
• Energy: Conduct couplings at ambient temperature; employ microwave selectively to shorten reaction times and reduce energy demand.

Comparison table (general):

• Conventional: DMF or NMP; HATU/HBTU; DCM for washes.
• Greener alternative: 2-MeTHF or EtOAc/MeCN; EDC/Oxyma or DMTMM; cyclopentyl methyl ether (CPME) for extractions; ethanol for recrystallization.

Trade-offs:

• Solubility constraints of zwitterionic β-amino acids may necessitate polar aprotic solvents; evaluate aqueous/bi-phasic systems or form salts to improve compatibility with greener media.

Pharmaceutical Uses

No pharmacopeial status or excipient designation is provided for this item.

General formulation context (literature/general):

• Amino acids can function as stabilizers, tonicity modifiers, or bulking agents in research-stage formulations (e.g., protein or peptide studies). β-amino acids are less common than α-amino acids for such roles.
• β-residues are used in peptidomimetic drug discovery to improve metabolic stability and adjust lipophilicity and target engagement. Any such use remains in the realm of research and development.

Important: This product is for research use only and is not intended for use in humans or for clinical applications. No therapeutic or clinical claims are made or implied.

Physical Properties

Item-specific physicochemical specifications (mp, bp, density, elemental limits, UV cutoff, water/peroxide/metal content) are not provided for this catalog entry.

• Melting point: Not specified for this item; refer to CoA/Spec Sheet.
• Boiling point: Not applicable (decomposes; amino acids generally do not distill intact) (literature/general).
• Density: Not specified for this item; refer to CoA/Spec Sheet.
• Solubility: Amino acids and β-amino acids are typically soluble in water under acidic/basic conditions; zwitterionic solids may exhibit moderate water solubility near the pI and enhanced solubility in dilute acid (e.g., 0.1–1 M HCl) or base (e.g., NaOH), and in polar aprotic solvents with added base (e.g., DMF/DMSO + Et3N) (literature/general). Item-specific solubility is not specified.
• pKa values: For β-amino acids, typical pKa ranges are ca. pKa1 (CO2H) ~2–3 and pKa2 (NH3+) ~9–10; exact values for DL-β-homoleucine are not specified for this item (literature/general).
• LogP/logD: Not specified for this item; refer to CoA/Spec Sheet. Hydrophobic side chain suggests lower aqueous solubility than unbranched β-amino acids at the isoelectric point (literature/general).
• Refractive index: Not applicable (solid) (general).

Note: For experimental values applicable to the supplied lot(s), consult the Certificate of Analysis (CoA) or Specification Sheet.

Quality and Grades

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

Guidance on grades for amino acid building blocks (general):

• Research grade: Suitable for synthetic and biochemical research. Purity often specified by HPLC/UPLC area% and/or titration; residual solvents/water by GC/KF; identity by NMR/HRMS.
• Peptide-synthesis grade: Emphasizes high chemical purity, low inorganic salts, and tight control of optical purity for enantiopure materials. For racemic DL materials, enantiomeric composition may be stated as DL = 1:1.
• Low-UV/LC-MS grade: If intended for analytical applications, low baseline and minimal nonvolatile impurities are important; this product has no such claim unless specified.

Stabilizers/additives:

• None indicated for this item. If present in certain lots (e.g., as salts), they will be disclosed on the CoA.

Quality documentation and testing:

• For lot-specific assays (purity, residual solvents, water content, metals, bioburden/endotoxin where applicable), and any peptide-synthesis suitability statements, consult the CoA/Spec Sheet. These parameters are not specified in this listing.

Reaction and Applications

DL-β-Homoleucine is a versatile building block for β-peptides, foldamers, and peptidomimetic scaffolds.

Applications (literature/general):

• Solid-phase and solution-phase synthesis of β-peptides and mixed α/β-peptides to tune helicity, proteolytic stability, and receptor selectivity.
• Structure–activity studies where leucine’s hydrophobicity is retained but the backbone spacing is increased by one methylene, altering bioactive conformations.
• Synthesis of β-amino acid-derived organocatalysts, amide isosteres, and small-molecule libraries.
• Preparation of amide-linked conjugates and dendrimers leveraging the amine and carboxylic acid bifunctionality.

Practical tips:

• Protecting groups: For orthogonal strategies, protect the β-amino group as Boc, Fmoc, or Cbz; the carboxyl as methyl/benzyl esters for solution work. Racemization is generally less problematic than for α-amino acids but monitor for epimerization at the stereocenter when applicable.
• Coupling: HATU/HBTU/EDC·HCl with HOAt/HOBt or Oxyma Pure in DMF/NMP; DIPEA or NMM as base. For hindered couplings, use COMU or activate as acid chloride/NHS ester under controlled conditions.
• Activation: Mixed anhydrides (isobutyl chloroformate) or CDI can be effective for mild amidations.
• Purification: Reverse-phase chromatography or ion-exchange. Salts may require desalting by lyophilization.

Analytical control:

• Monitor reactions by LC–MS and 1H NMR; quantify coupling completion by TNBS or Kaiser tests in SPPS (adapted for β-amino acids).

Reaction Conditions

Typical conditions for transformations of β-amino acids and peptide coupling (literature/general):

Amide bond formation (solution-phase):

• Solvent: DMF or NMP (0.05–0.2 M); greener alternatives include MeCN/EtOAc with DMTMM or aqueous EDC systems if soluble.
• Reagents: HATU (1.1–1.5 equiv) or EDC·HCl (1.2–2.0 equiv) + Oxyma/HOAt (0.1–1.0 equiv); base DIPEA or NMM (2–4 equiv).
• Temperature/time: 20–25°C, 0.5–16 h depending on partner sterics; monitor by LC–MS.

Solid-phase peptide synthesis (SPPS) with β-residue:

• Resin: Rink amide or Wang as appropriate.
• Coupling: 3–5 equiv β-amino acid (protected as Fmoc/Boc) + HBTU/HATU/COMU (3–5 equiv) + DIPEA in DMF; double coupling or extended times (20–60 min) can improve incorporation due to sterics.
• Deprotection: Fmoc removal with 20% piperidine/DMF; Boc final cleavage with TFA-based cocktails.

Functional group interconversions:

• Esterification: MeOH or iPrOH, catalytic acid (e.g., HCl(g) in MeOH) or DCC/DMAP; protect amine first to avoid salt formation.
• Reduction to β-amino alcohol: Borane–THF or LiAlH4 on protected derivatives; quench carefully; 0–25°C.
• β-lactam formation: Activate acid (e.g., acid chloride), intramolecular cyclization at dilute concentrations (≤0.01 M) with base (Et3N) in DCM/THF, 0–25°C.

Yields: Highly substrate- and method-dependent; consult primary literature for the target transformation. These conditions are general guidance only.

Safety and Handling

Hazard classification for this specific item is not provided; always consult the SDS.

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

General laboratory safety for amino acid solids (literature/general):

• Likely low acute toxicity but can cause mechanical irritation; avoid inhalation of dust and contact with eyes/skin.
• PPE: lab coat, safety glasses, and suitable gloves (e.g., nitrile). Use dust control (fume hood) during weighing.
• Incompatibilities: strong oxidizers, strong acids/bases can cause salt formation or decomposition on heating. Avoid mixing with nitrosating agents (amines can form N-nitroso species under harsh nitrosating conditions).
• Thermal behavior: typical amino acids char/decompose prior to boiling; avoid overheating and open flames.
• First aid (overview; refer to SDS):
  • Inhalation: move to fresh air; seek medical attention if symptoms persist.
  • Skin/eye contact: rinse with plenty of water; remove contaminated clothing; seek medical advice for persistent irritation.
  • Ingestion: rinse mouth; do not induce vomiting; seek medical attention if unwell.

Waste and spill: Collect solids by gentle sweeping/vacuum with HEPA; avoid dust generation. Dispose according to institutional and local regulations (non-halogenated organic/aqueous-compatible stream as appropriate).

Solvent Selection

As a zwitterionic β-amino acid with a hydrophobic side chain, DL-β-homoleucine displays solvent-dependent behavior typical of amino acids.

• Polarity/miscibility (literature/general):
  • Water: Often moderately soluble as the neutral zwitterion; markedly more soluble in acidic (e.g., dilute HCl) or basic media due to salt formation.
  • Alcohols: Limited solubility; can improve with slight acid/base to form salts.
  • Polar aprotics (DMF, DMSO, NMP): Good solubility, especially with a base (e.g., 0.1–1 equiv Et3N or DIPEA) to disrupt ionic pairing.
  • Nonpolar solvents (hexanes, toluene): Insoluble.

Selection tips:

• For peptide coupling and derivatization: DMF, NMP, or DCM/DMF mixtures are typical, with bases and coupling reagents to activate the carboxylate (literature/general).
• For preparative handling/stock solutions: Use water adjusted to pH 2–3 (HCl) or pH 9–10 (NaOH) to maximize solubility; filter sterilize if sterile solutions are needed for biochemical assays.
• For chromatographic purification: Reverse-phase systems (water/acetonitrile + 0.1% TFA, FA, or NH4HCO3) are commonly used for β-amino acids and short peptides; normal-phase often requires ion-pairing.

Comparison (general):

• β-amino acids with hydrophilic side chains dissolve more readily in water at neutral pH; hydrophobic side chains (like β-homoleucine) often require pH adjustment or polar aprotic solvents.

Storage and Reconstitution

• Storage conditions (product-specific): Room temperature.
• Shipped in: Not specified for this item; refer to CoA/Spec Sheet.

General guidance (literature/practice):

• Keep tightly closed in a dry container. Protect from excessive humidity and prolonged exposure to ambient light/heat.
• For long-term storage, a desiccator or dry cabinet is recommended to limit hygroscopic uptake and caking common to amino acid powders.

Reconstitution/solution preparation:

• Aqueous: Dissolve in water with pH adjustment (acidic or basic) to enhance solubility; filter sterilize if needed. Prepare fresh where possible.
• Organic: Use DMSO/DMF or alcohol–water mixtures; addition of a mild organic base (e.g., 0.1–0.5 equiv DIPEA) can aid dissolution.
• Storage of solutions: For best integrity, store aliquots at 2–8°C for short term or −20°C for longer term; avoid repeated freeze–thaw cycles. Actual stability is formulation- and pH-dependent; verify by LC–MS/HPLC.

Research Use Note: For research use only.

Structure and Identity

DL-β-Homoleucine is a racemic β-amino acid analogue of leucine, useful as a building block for β-peptides and peptidomimetics.

• CAS: 3653-34-7 (Product-specific)
• CID: 2733735 (Product-specific)
• InChIKey: Not specified for this item; refer to CoA/Spec Sheet.
• 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.

Structural features (general description):

• β-amino acid scaffold: a primary amine located on the β-carbon relative to the carboxylic acid (–NH2–CH(R)–CH2–CO2H pattern in one common representation), conferring increased backbone length versus α-amino acids.
• Side chain: leucine-like hydrophobic, branched alkyl substituent (isobutyl-type) attached to the β-backbone, providing pronounced hydrophobicity in peptides (literature/general).
• Stereochemistry: listed as DL (racemic), containing both enantiomers at the stereogenic center; no cis/trans alkene geometry.
• Functional groups: one carboxylic acid (weak acid), one primary amine (weak base); exists predominantly as a zwitterion near its isoelectric point (literature/general).

2D structure in words (general): a three-carbon backbone bearing a terminal carboxylate, with an amino substituent on the β-carbon and a branched hydrophobic side chain analogous to leucine attached to the same carbon that bears the amino group.

Synthetic Utility

Key functional elements of DL-β-homoleucine enable diverse transformations in synthetic and medicinal chemistry (literature/general):

• Bifunctional handle: Primary amine + carboxylic acid allow orthogonal derivatization to amides, esters, ureas, carbamates, and lactams.
• Peptide assembly: Serves as a β-residue in SPPS or solution synthesis; incorporation can modulate backbone geometry and hydrophobicity relative to leucine.
• Amide isosteres: Conversion to β-amino alcohols (via reduction) or β-lactams (via intramolecular cyclization) offers entry to constrained motifs.
• Side-chain chemistry: The branched hydrophobic side chain tolerates many conditions; selective side-chain oxidations or radical functionalizations can diversify libraries.
• Chiral resolution/derivatization: Although supplied as DL, diastereomeric salt formation (e.g., with chiral acids/bases) or chiral HPLC can provide enantiopure β-homoleucine for stereodefined studies.

Common named methods and tools:

• Coupling: HATU/HBTU/EDC + Oxyma; DMTMM for greener amidation.
• Protection: Boc/Fmoc/Cbz on amine; methyl/benzyl esters on acid. Hydrogenolysis (Cbz/Bn) or base/acid deprotection (Fmoc/Boc) under standard conditions.
• Activation: Mixed anhydrides (isobutyl chloroformate), NHS esters, CDI-mediated couplings.
• Cyclization: Formation of β-lactams via intramolecular acylation of the amino group after activation under high dilution.

Analytics: LC–MS, 1H/13C NMR, and chiral HPLC for enantiomeric profiling; titration for acid/base equivalence.

Target Specificity

Not applicable. This product is a small-molecule amino acid building block, not a biological affinity reagent or antibody. No antigen/epitope specificity, clone, isotype, or species reactivity applies.