Fmoc-O-allyl-D-tyrosine is a protected, derivatized amino acid in which the D-tyrosine core bears a phenolic side chain and an Fmoc-protecting group on the amino functionality, classifying it as an Fmoc-protected amino acid building block for peptide chemistry. The phenolic hydroxyl is converted to an O-allyl ether, while the molecule retains a free carboxyl group, giving it both an Fmoc-controlled amine reactivity profile and an allyl-protected phenol that can be removed under appropriate deprotection conditions to restore the tyrosine functionality. In synthetic workflows, it is employed as a stepwise coupling substrate for incorporating D-tyrosine into peptides or peptide-related intermediates and as a chemically defined precursor for preparing tyrosine-containing analogues for structure-activity studies, labeling, or biomolecular conjugation strategies.
CAT No: CP02118
Fmoc-O-allyl-D-tyrosine is an Fmoc-protected, D-configured tyrosine derivative in which the phenolic hydroxyl is masked as an O-allyl ether, yielding a stable amino acid building block for solid-phase peptide synthesis and orthogonal functionalization. The molecule combines an N-(9H-fluoren-9-ylmethoxycarbonyl) protecting group for controlled amide bond formation with a stereogenic amino acid center characteristic of D-tyrosine, enabling incorporation of D-configuration into peptide frameworks. The allyl ether on the side-chain phenol provides a handle for selective deprotection or functional transformation under conditions distinct from Fmoc removal. The aromatic phenyl ring and protected phenolic oxygen support downstream derivatization to phenolic, ether, or conjugatable tyrosine-like motifs while maintaining compatibility with peptide coupling chemistries.
1. Peptide Synthesis
Fmoc-O-allyl-D-tyrosine supports peptide building block preparation for automated solid-phase peptide synthesis, where Fmoc protection enables stepwise N-terminal deprotection and coupling. The amino acid backbone and carboxyl functionality are presented in a protected form suitable for standard peptide coupling strategies, while the D-tyrosine stereocenter supports incorporation of D-configuration into peptide sequences for stereochemical studies and analog construction. The O-allyl phenol masking allows temporary side-chain protection during chain assembly, reducing side reactions associated with free phenolic hydroxyls. Post-assembly, allyl removal or side-chain unmasking can generate tyrosine-like phenolic functionality for further derivatization, enabling access to peptide analogs used in structure-activity relationship studies and peptide science.
2. Side-Chain Functionalization
Fmoc-O-allyl-D-tyrosine is applied in synthetic organic chemistry for side-chain functionalization workflows that require orthogonal protection between the phenolic oxygen and the amino group. The allyl ether on the tyrosine phenol can be converted into phenolic or phenol-derived functionalities through selective deprotection and subsequent functional group interconversions, while the Fmoc group remains stable under many derivatization conditions. The aromatic ring and phenoxy oxygen arrangement supports targeted generation of conjugation-ready handles for building peptidomimetics, fluorescent tags, or affinity-ligand precursors. The D-stereochemistry can be retained to probe stereochemical effects on binding and reactivity, making the compound suitable for controlled generation of D-tyrosine-containing derivatives.
3. Peptidomimetics And SAR
Fmoc-O-allyl-D-tyrosine serves as a chiral input for peptidomimetic construction and SAR studies where D-amino acid incorporation is used to modulate conformational preferences and proteolytic stability profiles. The Fmoc-protected N-terminus enables rapid assembly of analog libraries, while the protected phenolic side-chain helps maintain consistent chemistry across series during synthesis and purification. The allyl-protected hydroxyl supports uniform handling of the tyrosine side chain, followed by controlled unmasking to install phenol-dependent motifs such as ether substituents or phenol-reactive intermediates. Downstream analogs derived from this building block can be used to generate structure-defined molecular scaffolds for comparative studies of stereochemistry and side-chain electronics in amino acid derivative research.
4. Bioconjugation Chemistry
Fmoc-O-allyl-D-tyrosine is utilized in chemical biology and bioconjugation chemistry as a protected tyrosine precursor for generating conjugation-ready phenolic or phenoxy-reactive intermediates. The protected phenolic oxygen enables storage and handling without uncontrolled oxidation or crosslinking during precursor synthesis, while allyl masking provides a controllable trigger for later exposure of the phenol. The D-tyrosine stereocenter supports stereodefined labeling strategies that can be important for receptor-binding assays, affinity probes, and stereospecific biomolecule modification. The resulting tyrosine-functionalized products can be incorporated into peptide conjugates or used as intermediates for attaching biomolecular recognition elements in applied biochemical research.
5. Pharmaceutical Manufacturing Intermediates
Fmoc-O-allyl-D-tyrosine can be employed in pharmaceutical manufacturing and process chemistry contexts as a protected amino acid intermediate for producing D-tyrosine-containing peptide intermediates. The combination of Fmoc protection and O-allyl side-chain protection aligns with manufacturing needs for predictable chemoselectivity during peptide coupling and controlled deprotection steps. The aromatic phenol masking reduces variability from side reactions during scale-up of protected amino acid handling, while the D-configuration supports stereochemically defined downstream intermediates used in fine chemical production. The compound's structure thus supports reliable conversion into peptide building blocks and protected derivatives that can be further processed into stereodefined molecular entities for industrial peptide and specialty chemical manufacturing workflows.
1. Peptides as Active Ingredients: A Challenge for Cosmeceutical Industry
5. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
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