L-Cyclohexylalanine is a natural, proteinogenic amino acid featuring a cyclohexyl side chain attached to the alpha carbon, with the amino acid backbone bearing a primary amino group and a carboxyl group. The molecule is in the L stereochemical form as indicated by the name, and its bulky, hydrophobic cyclohexyl substituent provides nonpolar character while remaining compatible with peptide-forming transformations at the amino and carboxyl functionalities. L-Cyclohexylalanine is used in peptide synthesis and structure-activity or protein-engineering studies where incorporation of a sterically demanding, hydrophobic side chain is used to probe sequence effects, conformational preferences, and intermolecular interactions.
CAT No: CP21003
CAS No:27527-05-5
Synonyms/Alias:(S)-2-amino-3-cyclohexylpropanoicacid;27527-05-5;L-Cyclohexylalanine;L-3-Cyclohexylalanine;3-Cyclohexyl-L-alanine;BETA-CYCLOHEXYL-ALANINE;(2S)-2-amino-3-cyclohexylpropanoicacid;(S)-2-Amino-3-cyclohexylpropionicacid;CHEMBL383208;SBB065823;Cyclohexylalanine;3-cyclohexylalanine;2-AMINO-3-CYCLOHEXYL-PROPIONICACID;beta-cyclohexylalanine;PubChem5760;AC1LEHTM;L-beta-Cyclohexylalanine;AC1Q5QKA;Maybridge4_003592;SCHEMBL123134;AC1Q4U81;MolPort-000-146-220;ORQXBVXKBGUSBA-QMMMGPOBSA-N;HMS1531D06;ANW-75380
L-Cyclohexylalanine is an L-configured amino acid featuring a chiral α-carbon linked to an amino group and a carboxylic acid, with a cyclohexyl side chain that is predominantly hydrophobic and conformationally constrained. The side-chain cyclohexyl ring provides steric bulk and shape-defined interactions that can influence peptide secondary structure, folding propensity, and binding-site complementarity. As a standard amino acid scaffold, it participates in conventional amide bond formation via carboxyl activation and can be incorporated as a residue in peptide building blocks after appropriate protection of the amino and/or carboxyl functionality. The amino acid's functional group set supports derivatization to esters, protected amino acid intermediates, and downstream chiral synthetic targets for both biochemical research and industrial fine chemical workflows.
1. Peptide Synthesis
L-Cyclohexylalanine is used in peptide synthesis as an L-amino acid residue for constructing hydrophobic segments in linear peptides and peptide fragments. The α-amino and α-carboxyl groups enable peptide coupling after conversion to protected amino acid forms, while the cyclohexyl side chain can modulate local conformation and improve compatibility with standard coupling chemistries. Incorporation into protected peptide sequences supports sequential chain assembly and enables downstream deprotection steps to reveal the native residue for further functionalization. L-Cyclohexylalanine thus functions as a structural element for peptide building block preparation and peptidomimetic scaffold generation in research-grade synthesis.
2. Chiral Building Block Development
L-Cyclohexylalanine serves as a chiral amino acid intermediate for stereodefined synthesis of substituted cyclohexyl-containing motifs and amino acid-derived chiral fragments. The L-configuration at the α-carbon provides a defined stereochemical handle that can be retained through derivatization to esters, amides, or protected amino acid derivatives used in asymmetric or stereospecific transformations. Side-chain cyclohexyl geometry can be leveraged to access conformationally restricted intermediates for medicinal chemistry-style fragment elaboration and chiral pool strategies. Downstream utilization includes preparation of stereochemically consistent intermediates for chemical manufacturing and fine chemical synthesis where cyclohexyl-substituted scaffolds are required.
3. Amino Acid Derivatization
L-Cyclohexylalanine is suitable for amino acid derivatization workflows that generate esters, N-protected derivatives, and carboxyl-activated intermediates for controlled downstream coupling. The free carboxylic acid can be converted into activated forms for amide formation, while the amino group can be protected to enable selective transformations on the side chain or controlled peptide incorporation. Cyclohexyl side-chain hydrophobicity can support the design of lipophilic analogs used in chemical biology probes, substrate mimics, and labeling reagents that require stable, nonpolar residue characteristics. Resulting derivatives can be employed as process chemistry intermediates for manufacturing routes that rely on protected amino acid chemistry and predictable functional group reactivity.
4. Chemical Biology Probes
L-Cyclohexylalanine can be incorporated into chemical biology constructs where hydrophobic, conformationally constrained residues are used to tune molecular recognition and membrane-associated behavior. The amino acid backbone supports incorporation into peptide-based probes, while the cyclohexyl side chain can influence binding-site hydrophobic contacts and help define the spatial presentation of neighboring functional groups. N- or C-terminal modification strategies can be applied after protecting-group selection to enable conjugation to tags, linkers, or reporter moieties for biochemical investigation. The compound's residue-level compatibility with peptide coupling chemistry makes it applicable for probe synthesis, enzyme substrate analog design, and structure-guided molecular interrogation.
5. Pharmaceutical Intermediate Preparation
L-Cyclohexylalanine is used in pharmaceutical intermediate preparation as a chiral building block for generating amino acid-derived fragments, hydrophobic peptide-like motifs, and stereochemically defined intermediates used in medicinal chemistry manufacturing. The cyclohexyl side chain provides a nonpolar, conformationally restricted element that can be carried through protecting-group strategies and coupling steps to form amide linkages in larger synthetic sequences. Protected amino acid derivative preparation enables controlled assembly of peptidomimetic structures and supports downstream purification and handling in industrial fine chemical synthesis. The resulting intermediates can feed into broader synthetic programs requiring consistent stereochemistry and reliable functional group interconversion for applied product development.
6. Analytical Research Standards
L-Cyclohexylalanine can serve as an analytical research standard or reference material for method development in amino acid profiling, peptide hydrolysate analysis, and chiral analysis workflows. The defined L-stereochemistry and characteristic cyclohexyl side chain improve chromatographic and spectrometric distinguishability relative to other amino acid residues. Derivatization to detectable forms, including derivatized esters or N-protected analogs, can support targeted quantification and confirm identity during peptide synthesis and downstream processing. Use in analytical research aligns with amino acid chemistry quality control needs and supports reliable interpretation of peptide construction and intermediate formation across synthetic and biochemical studies.
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