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Specifications
| Appearance | White powder |
| Purity (HPLC) | 98% min |
| Optical Purity | Report |
| Specific Rotation [α]20/D | Report -47.6° (C=2 in EtOH) |
| Melting Point | Report 163.2–164.6 ℃ |
| Clarity of solution | 0.3 gram in 2 ml DMF clear solution |
| Water Content (K.F.) | 1.0% max |
| Loss on drying | 2.0% (50°C 2h) max |
| IR Spectrum | In accordance with the structure |
| Mass Spectrum | In accordance with the structure |
| NMR Spectrum | In accordance with the structure |
Applications
Fmoc-2-chloro-L-phenylalanine (CAS 198560-41-7) is a protected amino acid widely used as a building block in solid-phase peptide synthesis (SPPS) and peptide-based research. The Fmoc (9-fluorenylmethyloxycarbonyl) protecting group allows selective N-terminal protection, facilitating stepwise assembly of peptides while preventing unwanted side reactions. The 2-chloro substitution on the phenylalanine aromatic ring introduces electron-withdrawing and steric effects, which can modulate peptide conformation, stability, and biological activity. This amino acid is commonly applied in the synthesis of bioactive peptides, peptide-based drugs, and modified peptides for medicinal chemistry studies, including receptor binding optimization and structure–activity relationship (SAR) investigations. It is also used in academic research and chemical biology to prepare fluorescently labeled or functionalized peptides for biochemical assays.
Benefits
The benefits of Fmoc-2-chloro-L-phenylalanine come from its chemical stability, stereochemical purity, and versatility in peptide design. The Fmoc group allows mild deprotection under basic conditions without affecting sensitive functional groups, enabling high-efficiency peptide synthesis. The chloro substitution provides enhanced control over peptide secondary structure and can improve metabolic stability or receptor selectivity in bioactive sequences. Its high optical purity ensures reproducible incorporation into peptides with precise stereochemistry, which is critical for biological function. Furthermore, it is compatible with standard SPPS protocols and common coupling reagents, facilitating scalability from laboratory research to industrial peptide manufacturing.
Conclusion
Fmoc-2-chloro-L-phenylalanine is a valuable protected amino acid for peptide synthesis and medicinal chemistry applications. Its combination of Fmoc protection, stereochemical integrity, and 2-chloro substitution allows precise peptide assembly, structural modulation, and functional optimization. By supporting efficient, high-quality synthesis of bioactive and modified peptides, Fmoc-2-chloro-L-phenylalanine remains an important tool in research, drug development, and peptide-based innovation.
