Cbz-3-Methy-D-Phenylalanine is a Cbz-protected, non-natural amino acid derivative featuring a D-phenylalanine backbone bearing a 3-methyl substituent on the aromatic side chain. The molecule contains both amino and carboxyl functionalities, with the amino group masked as a benzyloxycarbonyl (Cbz) carbamate that reduces undesired side reactions during coupling chemistry. In peptide synthesis workflows, this protected analogue functions as a stepwise building block for introducing the sterically and electronically modified 3-methyl phenylalanine residue into peptides or peptide-related intermediates, while the D stereochemical configuration is retained from the supplied structure.
CAT No: CP15709
Cbz-3-Methy-D-Phenylalanine is a Cbz-protected, stereodefined amino acid derivative in which the D-configuration at the alpha carbon is retained during peptide coupling chemistry. The molecule contains a benzyloxycarbonyl (Cbz) carbamate on the amino functionality, a free carboxyl group suitable for activation to peptide-forming derivatives, and a side chain featuring a 3-methyl substituted phenyl ring that modulates hydrophobicity and steric profile. The aromatic side chain can participate in π-π and hydrophobic interactions in peptide analogs, while the Cbz protecting group provides orthogonal stability under many peptide synthesis conditions and can be removed by hydrogenolysis when deprotection is required. As a chiral amino acid intermediate, Cbz-3-Methy-D-Phenylalanine is designed to support stereocontrolled incorporation into peptides and to enable downstream functionalization through carboxyl activation and side-chain-directed synthetic elaboration.
1. Peptide Synthesis
Cbz-3-Methy-D-Phenylalanine is applied in peptide building workflows where a D-amino acid residue is required to tune conformational preferences and protease resistance profiles in peptide science. The Cbz-protected amine and carboxylic acid enable standard peptide coupling strategies after conversion of the acid to an activated species, supporting stepwise assembly of protected peptide chains. The D-stereocenter and 3-methyl phenyl side chain provide defined stereochemical and steric elements that influence amide bond geometry and side-chain packing. Peptide building block preparation and subsequent deprotection steps can be coordinated by the Cbz group's selective removal behavior, supporting the synthesis of D-residue-containing peptides and peptidomimetic scaffolds.
2. Peptidomimetics And SAR
Cbz-3-Methy-D-Phenylalanine is utilized in structure-activity relationship studies and peptidomimetic construction where aromatic side-chain substitution and D-configuration are used to modulate binding interactions. The 3-methyl substituted phenyl ring supports controlled hydrophobic surface area and steric bulk, while the D-alpha stereochemistry can shift backbone orientation relative to L-analogues. The Cbz carbamate protects the amino terminus during scaffold assembly, allowing systematic substitution patterns across a peptide-like framework without premature amine reactivity. Incorporation into analog series supports downstream generation of structure-defined derivatives for SAR mapping, including analogs bearing altered spacing, conformational constraints, or side-chain modifications.
3. Chemical Biology Labeling
Cbz-3-Methy-D-Phenylalanine is suitable for chemical biology research that requires incorporation of a chiral, protected amino acid residue into functional peptide probes. The protected amine (Cbz) and carboxyl handle allow the residue to be integrated into peptide conjugates that can later be functionalized at termini or through subsequent side-chain derivatization routes. The aromatic side chain can serve as a hydrophobic anchor within probe designs, improving compatibility with binding pockets or membrane-associated targets in assay formats. Hydrogenolytic removal of the Cbz group can be used to unmask the amine for further conjugation steps, enabling the preparation of labeled biomolecule fragments and peptide-based reagents for molecular recognition studies.
4. Protected Amino Acid Chemistry
Cbz-3-Methy-D-Phenylalanine is employed as a chiral protected amino acid intermediate for orthogonally managed synthesis planning in fine chemical and peptide manufacturing contexts. The Cbz protecting group provides a stable carbamate during coupling and chain elongation, while the D-configuration at the alpha carbon supports stereochemical fidelity for downstream peptide assembly. The free carboxylic acid functionality can be converted to peptide-grade intermediates for controlled amide formation, supporting reproducible manufacturing routes for protected peptide building blocks. The defined aromatic side chain substitution enables consistent incorporation into libraries of protected residues, supporting batch-to-batch reproducibility in amino acid derivative preparation and downstream peptide construction.
5. Process Chemistry Intermediate
Cbz-3-Methy-D-Phenylalanine is applied as a chiral intermediate in process chemistry for producing D-amino acid-containing peptide fragments and related specialty chemicals. The presence of a single, removable Cbz carbamate and a carboxylic acid group supports scalable conversion to activated coupling forms and subsequent peptide bond formation under controlled conditions. The stereodefined D-center and 3-methyl phenyl substituent reduce ambiguity in downstream structure specification, which is important for manufacturing of stereochemically consistent intermediates. The compound's compatibility with peptide synthesis workflows makes it suitable for industrial fine chemical synthesis where protected amino acid handling, selective deprotection, and downstream derivatization are integrated into a coherent process chain.
6. Analytical Standard Development
Cbz-3-Methy-D-Phenylalanine is used for analytical research and method development as a stereochemically defined reference material for amino acid derivative profiling. The Cbz-protected structure and aromatic side chain substitution provide distinct chromatographic and mass spectrometric signatures, supporting identification of D-residue-containing intermediates and monitoring of deprotection or coupling completeness. The defined functional groups allow the compound to serve as a calibration or comparison standard when analyzing protected amino acid building blocks, partially protected peptides, or hydrolysis products. Chiral specificity arising from the D-configuration and the 3-methyl phenyl substitution supports accurate interpretation in analytical workflows focused on stereochemical integrity during peptide synthesis and amino acid derivatization.
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