N-Fmoc-4-chloro-L-homophenylalanine carries a chlorine-modified aromatic extension that influences hydrophobic interactions and side-chain volume. The residue supports studies of stacking behavior, backbone orientation, and conformational energetics. Researchers apply it to engineer peptides with tuned aromatic character. Its Fmoc group ensures predictable synthetic behavior.
CAT No: R2120
CAS No:1260608-62-5
Synonyms/Alias:N-Fmoc-4-chloro-L-homophenylalanine;1260608-62-5;Fmoc-4-chloro-L-Homophe;(2S)-4-(4-chlorophenyl)-2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}butanoic acid;SCHEMBL21838005;MFCD07372182;BS-44806;CS-0187587;E74467;(2S)-4-(4-chlorophenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)butanoic acid;
N-Fmoc-4-chloro-L-homophenylalanine is a synthetic amino acid derivative characterized by the presence of an N-terminal fluorenylmethyloxycarbonyl (Fmoc) protecting group and a para-chloro substitution on the homophenylalanine side chain. As a non-canonical amino acid, it expands the toolkit available for peptide chemists and protein engineers seeking to introduce unique chemical functionalities into peptide sequences. Its structural modifications confer distinctive electronic and steric properties, making it an important tool for probing protein structure-function relationships, designing novel biomolecules, and advancing the development of peptide-based research applications.
Peptide synthesis: The compound is widely utilized as a building block in solid-phase peptide synthesis (SPPS), where the Fmoc group serves as a temporary protecting group for the α-amino function. Its incorporation enables the generation of peptides bearing a 4-chloro-substituted homophenylalanine residue, facilitating the design of analogs with altered hydrophobicity, aromatic interactions, or steric profiles. Researchers leverage such modifications to investigate structure-activity relationships, optimize peptide stability, or introduce bioorthogonal handles for downstream functionalization.
Structure-activity relationship studies: The unique side-chain properties imparted by the 4-chloro substituent allow for systematic exploration of how aromatic ring modifications affect peptide-protein or peptide-receptor interactions. By incorporating this amino acid analog into specific sequence positions, scientists can dissect the contributions of hydrophobicity, electronic effects, and steric bulk to binding affinity, selectivity, or biological recognition in model systems or target peptides.
Peptide-based probe development: The distinct chemical features of the chloro-substituted homophenylalanine residue make it valuable for the design of specialized peptide probes. Such probes are employed in biochemical assays, molecular recognition studies, or affinity purification protocols, where the altered aromatic side chain can modulate target binding or serve as a unique epitope for detection and labeling strategies.
Enzyme substrate specificity research: The introduction of non-standard amino acids like 4-chloro-L-homophenylalanine into peptide substrates provides a means to investigate enzyme specificity and catalytic mechanisms. By substituting this residue at key positions within peptide substrates, researchers can assess the tolerance of proteases, peptidases, or other enzymes to side-chain modifications, thereby elucidating active site preferences, substrate scope, and structure-function correlations.
Peptidomimetic and drug discovery efforts: The compound is also applied in the generation of peptidomimetics and lead optimization campaigns, where the incorporation of non-proteinogenic amino acids can enhance metabolic stability, modulate conformational preferences, or improve pharmacological properties. Its unique side-chain features enable the design of novel peptide analogs with tailored physicochemical attributes for high-throughput screening or mechanistic investigations in preclinical research settings.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More