N-Fmoc-4-chloro-D-homophenylalanine incorporates an extended aromatic side chain bearing a chlorine substituent that alters electron density and hydrophobic packing. The D-configuration introduces stereochemical contrast for structural studies. Researchers use it to modulate aromatic interactions and probe conformational restrictions. Its Fmoc protection supports incorporation into synthetic peptide assemblies.
CAT No: R2150
CAS No:1260590-79-1
Synonyms/Alias:N-Fmoc-4-chloro-D-homophenylalanine;1260590-79-1;F80650;(2R)-4-(4-chlorophenyl)-2-(9H-fluoren-9-ylmethoxycarbonylamino)butanoic acid;(R)-2-((((9H-Fluoren-9-yl)methoxy)carbonyl)amino)-4-(4-chlorophenyl)butanoic acid;
N-Fmoc-4-chloro-D-homophenylalanine is a synthetically modified, non-proteinogenic amino acid derivative featuring a fluorenylmethyloxycarbonyl (Fmoc) protecting group and a para-chloro substitution on the homophenylalanine backbone. As a chiral amino acid analogue, it is commonly utilized in peptide chemistry and advanced synthetic protocols due to its unique combination of steric and electronic properties. The presence of both the D-configuration and the 4-chloro substitution imparts distinct conformational and physicochemical characteristics, making it a valuable building block for the construction of specialized peptides and peptidomimetics. Its structural features enable researchers to modulate peptide folding, stability, and bioactivity in a controlled manner, supporting diverse investigations in chemical biology and medicinal chemistry.
Peptide synthesis: N-Fmoc-4-chloro-D-homophenylalanine is widely employed as a protected amino acid monomer for solid-phase peptide synthesis (SPPS) and solution-phase protocols. The Fmoc group provides orthogonal protection for the α-amino function, allowing for efficient stepwise assembly of peptide chains under mild deprotection conditions. The 4-chloro substituent on the aromatic ring can influence the hydrophobicity and steric profile of the resulting peptide, enabling the design of sequences with tailored conformational preferences or altered side chain interactions. Researchers use this derivative to incorporate non-canonical residues into synthetic peptides, expanding the chemical diversity accessible for structure-activity relationship studies.
Peptidomimetic design: The incorporation of D-homophenylalanine analogues bearing halogen substituents is a strategic approach in the design of peptidomimetics with enhanced metabolic stability and resistance to proteolytic degradation. The D-configuration disrupts recognition by endogenous proteases, while the 4-chloro group further modifies the electronic environment of the side chain, potentially affecting binding interactions with target proteins. Such modifications are crucial in the development of peptide-based probes, inhibitors, and scaffolds for probing biological pathways or modulating protein-protein interactions.
Conformational analysis: N-Fmoc-4-chloro-D-homophenylalanine serves as a tool for investigating peptide secondary structure and conformational dynamics. Its extended side chain and aromatic substitution can promote or disrupt specific folding motifs, such as β-turns or helices, depending on sequence context. By systematically incorporating this residue into model peptides, researchers can study the effects of side chain modifications on backbone flexibility, intramolecular interactions, and overall structural stability using spectroscopic or crystallographic techniques.
Structure-activity relationship (SAR) studies: The unique steric and electronic features of this amino acid analogue make it valuable for SAR investigations in peptide-based research. By substituting canonical residues with N-Fmoc-4-chloro-D-homophenylalanine, scientists can systematically assess the impact of side chain modifications on biological activity, target affinity, or selectivity. Such studies are essential for optimizing lead compounds in early-stage discovery projects or exploring the molecular determinants of bioactive peptide function.
Analytical method development: The distinct chemical properties of N-Fmoc-4-chloro-D-homophenylalanine, including its UV-active Fmoc group and halogenated aromatic ring, facilitate its detection and quantification in analytical workflows. It can be used as a reference standard or as a probe in chromatographic and spectroscopic method development, supporting quality control of synthetic processes or characterization of complex peptide mixtures. The presence of the chloro substituent also enables site-specific derivatization or labeling strategies for advanced analytical applications.
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