3-Chloro-D-tyrosine is a halogenated, non-proteinogenic amino acid derivative featuring a D-configured amino acid backbone bearing a phenolic aromatic side chain substituted with a chlorine at the 3-position. The molecule contains both an amino group and a carboxylic acid group, and its chlorinated phenol provides distinct electronic and hydrogen-bonding characteristics compared with unsubstituted tyrosine while maintaining the aromatic ring functionality associated with tyrosine-like side chains. In chemical biology and peptide chemistry, this compound is used as a defined building block for incorporating a sterically and electronically modified tyrosine analogue into synthetic peptides and for preparing labeled or reactive aromatic handles in structure-activity studies, conjugation workflows, and analytical method development.
CAT No: CP17702
3-Chloro-D-tyrosine is a D-configured tyrosine analog bearing a chloro substituent on the aromatic ring, providing a halogenated phenolic amino acid scaffold for chemical biology and peptide chemistry workflows. The presence of the phenolic side chain supports derivatization and controlled functionalization, while the C-Cl substituent offers a distinct electronic and steric profile compared with unmodified tyrosine. As a non-proteinogenic amino acid building block, it is commonly used to introduce halogenated aromatic motifs into peptides and to generate site-distinct standards for analytical and SAR-focused studies.
1. Halogenated Peptide Building Block
3-Chloro-D-tyrosine is used by peptide synthesis teams to incorporate a halogenated aromatic residue into custom peptides and peptidomimetics where the D-configuration and chlorinated phenyl ring are required for stereochemical control, conformational effects, or to tune physicochemical properties. Researchers developing protease-stability or structure-activity relationship (SAR) libraries often select this residue to create analog series that differ specifically at the aromatic substitution pattern, enabling downstream comparative evaluation of peptide behavior in biochemical assays. The phenolic side chain also provides a handle for further modification of the aromatic functionality during or after assembly, supporting workflows that require controlled side-chain chemistry rather than relying on unmodified tyrosine.
2. Chemical Biology Probe Residue
3-Chloro-D-tyrosine is applied in chemical biology and protein chemistry as a non-natural amino acid residue for building probes and functionalized peptide ligands that carry a site-distinct aromatic motif. Teams studying aromatic recognition, binding-site microenvironments, or residue-specific effects frequently use halogenated tyrosine analogs to create labeling reagents or peptide-based tools with altered sterics and electronics at the phenyl ring. The D-configuration helps ensure that the residue is not treated as a native stereochemical match, which is valuable when researchers need a chemically defined, non-proteinogenic substitution for mapping, competition experiments, or mechanistic studies using synthetic peptide constructs.
3. Medicinal Chemistry SAR Intermediate
3-Chloro-D-tyrosine is used in medicinal chemistry programs as a defined chiral amino acid intermediate for preparing halogenated tyrosine-derived motifs within larger synthetic sequences. Medicinal chemistry and process development groups often rely on such chlorinated aromatic building blocks to access analogs used in SAR campaigns, where the position-specific C-Cl substitution is a key variable for tuning properties like hydrophobicity and aromatic interaction patterns. The phenolic functionality supports conversion into downstream derivatives required for coupling, protection/deprotection strategies, or further functional group elaboration, making this residue a practical starting point for constructing halogenated aromatic pharmacophore fragments.
4. Analytical Standard Preparation
3-Chloro-D-tyrosine is also used for analytical method development and reference material preparation in workflows that require a chemically distinct tyrosine analog. Laboratories performing LC-MS-based quantification, peptide profiling, or targeted analysis of synthetic peptide components may use the chlorinated D-tyrosine residue as a structural standard to verify retention behavior and fragment patterns for halogenated aromatic species. Because the compound differs from native tyrosine by both stereochemistry and aromatic substitution, it provides an unambiguous reference point when researchers need to separate signals arising from unmodified amino acids or closely related tyrosine derivatives.
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