Fmoc-D-Homocys(Trt)-OH is an Fmoc-protected, D-configured homocysteine-derived amino acid derivative featuring an extended thioether side chain and a carboxylic acid suitable for peptide-coupling chemistry. The molecule contains an N-terminal 9H-fluoren-9-ylmethoxycarbonyl (Fmoc) protecting group on the amino functionality and a trityl (Trt) protecting group on the side-chain sulfur, while retaining the free α-amino and α-carboxyl functional groups for controlled assembly of peptide intermediates. In synthesis, this protected amino acid is employed as a building block in stepwise peptide synthesis to manage chemoselectivity of the thioether-containing residue and to support the preparation of labeled or structurally modified peptides and peptide analogues for chemical biology and analytical studies.
CAT No: CP26125
CAS No:1007840-62-1
Synonyms/Alias:(R)-2-(Fmoc-amino)-4-tritylsulfanyl-butyric acid
Fmoc-D-Homocys(Trt)-OH is an Fmoc-protected D-homocysteine derivative bearing a Trt (trityl) protected thiol side chain, providing a stable, chiral amino acid building block for peptide chemistry. The molecule contains an Fmoc carbamate on the α-amino group and a carboxylic acid at the C-terminus, while the side chain sulfur is masked as a Trt thioether/thiol-protecting group that suppresses oxidation and unwanted disulfide formation during coupling. The D-stereochemistry at the α-carbon enables stereochemically defined incorporation into peptide sequences and peptidomimetic scaffolds. The combination of orthogonal protection and a protected thiol functional handle supports downstream deprotection to regenerate a reactive thiool for selective conjugation, cyclization, or thiol-based ligation chemistry.
1. Peptide Synthesis
Fmoc-D-Homocys(Trt)-OH is suited for solid-phase peptide synthesis and automated peptide assembly where orthogonal protection is required for side-chain thiol handling. The Fmoc group enables base-mediated removal to expose the α-amine for iterative peptide coupling, while the Trt-protected homocysteine thiol remains inert under standard coupling and washing conditions. The carboxylic acid participates in amide bond formation using common peptide coupling strategies, and the D-configuration supports stereodefined peptide backbones for unnatural amino acid incorporation. After sequence assembly, Trt removal can generate a free thiol for subsequent steps such as disulfide formation, thioether installation, or cyclization. The resulting peptide products can be used as research-grade ligands, enzyme probes, or scaffold elements where controlled sulfur chemistry is required.
2. Bioconjugation Chemistry
Fmoc-D-Homocys(Trt)-OH supports bioconjugation workflows that rely on site-defined sulfur reactivity after controlled deprotection. The protected thiol functionality allows incorporation into peptide or protein fragments without premature oxidation, while the D-homocysteine side chain provides a chemically distinct handle for thiol-directed labeling or conjugation chemistry. Fmoc protection provides compatibility with peptide fragment synthesis, enabling downstream generation of thiol-bearing conjugates through Trt deprotection under conditions that preserve other functional groups. The carboxylic acid and amide-forming capacity facilitate attachment to targeting motifs, linkers, or affinity tags in a modular manner. The compound therefore functions as a chiral, protected amino acid intermediate for constructing sulfur-containing conjugates used in chemical biology and analytical reagent development.
3. Peptidomimetics And SAR Studies
Fmoc-D-Homocys(Trt)-OH can be applied to peptidomimetic construction and structure-activity relationship studies where sulfur-containing side chains influence conformational preferences and binding interactions. The D-homocysteine stereocenter and protected thiol enable incorporation into analog libraries while maintaining chemical stability during synthesis and purification. The Fmoc strategy supports rapid assembly of analog series, and the Trt group provides a controlled pathway to introduce free thiol for thioether formation, disulfide constraints, or sulfur-based crosslinking. The resulting peptidomimetic scaffolds can be used to probe how side-chain sulfur substitution patterns affect molecular recognition and stability in biochemical assays. The compound's protection pattern aligns with synthetic methodology development focused on amino acid derivatization and controlled functional group presentation.
4. Chemical Manufacturing Intermediates
Fmoc-D-Homocys(Trt)-OH serves as a process-relevant intermediate for producing protected amino acid derivatives and thiol-functional peptide building blocks on industrial scales. The Fmoc carbamate and Trt-protected thiol provide robust chemical handles that can be carried through multi-step manufacturing sequences with minimized side reactions such as thiol oxidation and disulfide scrambling. The presence of a free carboxylic acid supports conversion into activated ester or coupling-ready derivatives during downstream intermediate preparation, enabling integration into manufacturing routes for peptide reagents and fine chemicals. The stereochemically defined D-center supports consistent batch-to-batch structural fidelity for stereopure peptide fragments and sulfur-containing intermediates. The compound can therefore be employed in specialty chemical production where protected amino acid chemistry and reliable functional group masking are required for scalable synthesis.
5. Analytical Research Standards
Fmoc-D-Homocys(Trt)-OH can be used in analytical research for method development and reference material preparation involving sulfur-containing amino acid derivatives. The defined Fmoc-protected α-amino group and Trt-protected thiol create a reproducible chemical identity that supports LC-MS, HPLC, and peptide mapping workflows used to monitor protected amino acid synthesis and peptide coupling performance. The D-homocysteine stereochemistry enables discrimination from L analogs in stereospecific analytical contexts and supports the verification of stereochemical integrity in peptide building block inventories. Controlled deprotection to reveal thiol functionality can be integrated into analytical workflows that require thiol quantification or derivatization-based detection. The compound thus functions as a chiral, protected amino acid standard for biochemical research intermediate characterization and quality control-oriented studies.
1. High fat diet and GLP-1 drugs induce pancreatic injury in mice
2. Cationic cell-penetrating peptides are potent furin inhibitors
3. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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