Fmoc-3,5-Dimethy-D-Phenylalanine is an Fmoc-protected, non-natural phenylalanine derivative bearing a substituted aromatic side chain with two methyl groups at the 3 and 5 positions and a D stereochemical designation. The molecule contains a free carboxyl group and an Fmoc-protected amino functionality, with the aromatic ring providing hydrophobic character and steric modulation relative to unsubstituted phenylalanine. This protected amino acid is used as a building block for stepwise peptide synthesis and structure-activity studies where incorporation of a sterically biased, methyl-substituted phenylalanine analogue is required.
CAT No: CP14307
Fmoc-3,5-Dimethy-D-Phenylalanine is an Fmoc-protected D-phenylalanine derivative bearing two methyl substituents on the aromatic ring at the 3,5-positions, creating a sterically differentiated, hydrophobic side chain with defined stereochemistry at the alpha carbon. The molecule contains an Fmoc carbamate on the amino group, a free carboxyl functionality suitable for peptide coupling after activation, and a substituted benzyl side chain that can influence aromatic packing and conformational preferences in peptide backbones. The D-configuration supports incorporation of a non-proteinogenic stereochemical element, which can modulate protease recognition and alter local secondary-structure tendencies. The combination of an orthogonally removable Fmoc group and a substituted aromatic ring makes the compound a chiral amino acid intermediate for protected amino acid synthesis and downstream peptide or peptidomimetic construction.
1. Peptide Synthesis
Fmoc-3,5-Dimethy-D-Phenylalanine is used in peptide building block preparation for solid-phase peptide synthesis where the Fmoc carbamate enables iterative N-terminal chain elongation. The D-phenylalanine stereocenter and the 3,5-dimethyl-substituted aromatic side chain provide a controlled chiral residue that can be introduced as a single amino acid unit to tune sterics, hydrophobicity, and aromatic interactions in peptide sequences. The free carboxyl group participates in standard peptide coupling chemistry after activation, while the Fmoc group can be removed under base to expose the next coupling site without disturbing the aromatic methyl substituents. The resulting D-aromatic residue incorporation supports construction of peptide analogs for biochemical research, including sequence variants used to probe backbone recognition and structure-function relationships.
2. Peptidomimetics And SAR Studies
Fmoc-3,5-Dimethy-D-Phenylalanine is applicable to peptidomimetic construction and structure-activity relationship studies where aromatic side-chain substitution patterns are used to modulate binding-site contacts. The 3,5-dimethyl substitution on the phenyl ring can affect conformational bias and steric shielding, while the D-configuration can alter proteolytic stability and side-chain orientation relative to L-analogues. Fmoc protection supports incorporation into defined scaffolds, enabling systematic generation of analog libraries with consistent stereochemical control at the alpha carbon. The compound's protected amino acid format supports downstream derivatization of peptide fragments into optimized molecular scaffolds for SAR mapping and fragment-to-lead refinement workflows.
3. Chemical Biology Probes
Fmoc-3,5-Dimethy-D-Phenylalanine is suitable for chemical biology research requiring incorporation of non-natural stereochemistry and hydrophobic aromatic contrast into peptide-based probes. The substituted phenyl ring can serve as a handle for hydrophobic and π-interaction-driven recognition in target-binding assays, while the D-amino acid configuration provides a stereochemical perturbation that can help distinguish probe behavior from native peptide substrates. The Fmoc group enables controlled assembly of probe peptides with defined length and residue positioning, and the carboxyl functionality supports coupling to linkers or further functional group transformations after peptide assembly. The resulting labeled or conjugatable peptide frameworks can be used to interrogate binding specificity, receptor engagement, or enzyme substrate preferences in biochemical studies.
4. Protein Engineering Workflows
Fmoc-3,5-Dimethy-D-Phenylalanine is relevant to protein engineering and in vitro protein modification strategies that incorporate D-amino acid residues into peptide domains. The Fmoc-protected amino acid format supports chemical synthesis of short engineered segments that can be ligated or conjugated to larger biomolecular constructs, enabling placement of the 3,5-dimethyl aromatic side chain at specific positions. The D-configuration can be used to influence local folding propensities and resistance to protease cleavage, which can be important when engineered peptides are used as binding modules or structural elements. The substituted aromatic residue can also provide a distinct physicochemical signature for studying conformational effects and interaction networks within protein-derived assemblies.
5. Pharmaceutical Intermediate Preparation
Fmoc-3,5-Dimethy-D-Phenylalanine is employed as a chiral amino acid intermediate in fine chemical synthesis for manufacturing peptide intermediates and peptidomimetic precursors. The Fmoc-protected amine and carboxyl functionality allow integration into protected amino acid synthesis routes that feed downstream peptide coupling steps, supporting reproducible handling of stereochemistry during scale-up. The 3,5-dimethyl-substituted aromatic side chain provides a defined hydrophobic motif that can be carried through manufacturing to generate specific intermediate structures for medicinal chemistry programs. Industrial workflows can leverage the orthogonal nature of Fmoc deprotection to design controlled conversion steps from protected building blocks to final peptide or peptide-like intermediates used in applied product development.
6. Analytical Standards to Peptide Profiling
Fmoc-3,5-Dimethy-D-Phenylalanine is useful for analytical research and method development where defined D-amino acid residues are needed as standards or internal references for peptide profiling. The compound's unique combination of D-stereochemistry and 3,5-dimethyl aromatic substitution creates a distinguishable mass and chromatographic signature compared with common phenylalanine derivatives. The Fmoc-protected form supports incorporation into synthetic peptide standards with known sequence context, enabling calibration of LC-MS/MS transitions and monitoring of residue-specific fragmentation patterns. The resulting reference materials can support quality control of peptide synthesis, characterization of peptide analogs, and verification of stereochemical incorporation in biochemical research workflows.
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