N-Fmoc-N-(cyclohexylmethyl)-glycine incorporates a bulky cyclohexylmethyl group, enhancing hydrophobic character and steric rigidity. The residue alters local folding and modulates backbone flexibility. Researchers use it to design constrained peptide frameworks and examine hydrophobic clustering. Its protected form facilitates controlled incorporation into synthetic sequences.
CAT No: R2143
CAS No:1374785-49-5
Synonyms/Alias:N-Fmoc-N-(cyclohexylmethyl)-glycine;1374785-49-5;[(cyclohexylmethyl)[(9H-fluoren-9-ylmethoxy)carbonyl]amino]acetic acid;MFCD31696121;CS-0439231;F80979;2-[cyclohexylmethyl(9H-fluoren-9-ylmethoxycarbonyl)amino]acetic acid;
N-Fmoc-N-(cyclohexylmethyl)-glycine is a synthetically modified amino acid derivative characterized by the presence of an N-terminal fluorenylmethyloxycarbonyl (Fmoc) protecting group and a cyclohexylmethyl substituent on the nitrogen atom of glycine. As a noncanonical amino acid, it serves as a versatile building block in peptide chemistry, enabling the introduction of steric bulk and hydrophobicity at specific positions within peptide chains. Its unique structure facilitates the exploration of side-chain modifications, conformational constraints, and physicochemical diversity in peptide and protein design, making it valuable for both academic and industrial research applications.
Peptide Synthesis: In solid-phase peptide synthesis (SPPS), N-Fmoc-N-(cyclohexylmethyl)-glycine is commonly employed as a protected amino acid monomer. The Fmoc group provides orthogonal protection, allowing for efficient stepwise elongation of peptide chains under mild deprotection conditions. Incorporation of the cyclohexylmethyl-modified glycine residue introduces steric hindrance and hydrophobic character, enabling researchers to tailor peptide conformation, modulate folding, and enhance resistance to enzymatic degradation. This makes it particularly useful for generating peptides with improved stability, altered biological properties, or novel structural motifs.
Peptidomimetic Design: The cyclohexylmethyl group on the nitrogen atom of glycine imparts significant conformational restriction, which is advantageous in the development of peptidomimetics. By mimicking the structural and functional aspects of natural peptides while increasing metabolic stability, such derivatives can be used to probe structure-activity relationships, investigate receptor binding interactions, and design analogs with enhanced bioavailability. The ability to introduce non-natural side chains expands the chemical space accessible for the rational design of peptide-based research tools and molecular probes.
Structure-Activity Relationship Studies: Researchers often utilize N-Fmoc-N-(cyclohexylmethyl)-glycine to systematically investigate the effects of side-chain modifications on peptide activity. By substituting conventional amino acids with this sterically demanding analog, it becomes possible to assess the impact on binding affinity, selectivity, and conformational dynamics in model peptides and protein fragments. Such studies provide essential insights for the optimization of peptide ligands, inhibitors, and scaffolds in biochemical research.
Protein Engineering: The incorporation of noncanonical amino acids like N-Fmoc-N-(cyclohexylmethyl)-glycine into synthetic peptide sequences supports the engineering of proteins with novel properties. By introducing bulky, hydrophobic side chains at specific sites, researchers can modulate protein-protein interactions, alter folding pathways, or stabilize particular secondary structures. This approach is instrumental in the development of artificial enzymes, molecular recognition elements, and advanced biomaterials with tailored functionalities.
Analytical and Method Development: The distinct physicochemical properties of N-Fmoc-N-(cyclohexylmethyl)-glycine make it a useful tool in analytical chemistry and method development. Its unique mass and hydrophobic profile facilitate the calibration of chromatographic systems, optimization of peptide purification protocols, and validation of analytical methods for modified peptides. Additionally, its incorporation into synthetic standards aids in the identification and quantification of structurally diverse peptide species during mass spectrometric or chromatographic analyses, supporting high-precision research in peptide science.
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