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Application Area

Fmoc-Cys(Trt)-O-DMP-4-OH

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

Fmoc-Amino Acids

Catalog number

BAT-008418

Application
Reference Reading

Fmoc-Cys(Trt)-O-DMP-4-OH, a specialized reagent utilized in peptide synthesis and bioconjugation, serves various purposes in the realm of biochemistry. Here are four key applications of Fmoc-Cys(Trt)-O-DMP-4-OH:

Solid-Phase Peptide Synthesis (SPPS): Embedded within the intricate world of SPPS, Fmoc-Cys(Trt)-O-DMP-4-OH emerges as a pivotal player, facilitating the integration of cysteine residues into peptides. The dual-guarding mechanism, involving the Fmoc (9-fluorenylmethyloxycarbonyl) group, shields the amine functionality, while the Trt (triphenylmethyl) group ensures the safeguarding of cysteine thiol, orchestrating selective reactions with unparalleled yield.

Protein Engineering: In the expansive domain of protein engineering, Fmoc-Cys(Trt)-O-DMP-4-OH emerges as a versatile tool, empowering the synthesis of cysteine-containing peptides that seamlessly integrate into larger protein frameworks. These cysteine entities play a pivotal role in the establishment of disulfide bonds, pivotal for stabilizing the structure and function of proteins. Researchers can wield this reagent with precision, strategically embedding these essential residues at targeted loci.

Drug Development: Embarking on the journey of drug development, peptides harboring cysteine become an indispensable asset, especially in sculpting therapeutic agents that target specific proteins or pathways. The precision offered by Fmoc-Cys(Trt)-O-DMP-4-OH in peptide synthesis ensures the creation of highly pure and precise cysteine-containing peptides. These peptides then serve as foundational blocks for further modifications or conjugations, augmenting their specificity and efficacy in therapeutic applications.

Bioconjugation: Delving into the realm of bioconjugation, the thiol group of cysteine emerges as a versatile linker, enabling the attachment of peptides to an array of molecules like fluorescent probes, enzymes, and drugs. Through the utilization of Fmoc-Cys(Trt)-O-DMP-4-OH, researchers can craft thiol-rich peptides that intricately bind to these functional groups in a selective manner. This pivotal step plays a crucial role in sculpting targeted therapeutics and diagnostic tools.

1. Stereoselective Polymer-Supported Synthesis of Morpholine- and Thiomorpholine-3-carboxylic Acid Derivatives

Petra Králová, Veronika Fülöpová, Michal Maloň, Tereza Volná, Igor Popa, Miroslav Soural ACS Comb Sci. 2017 Mar 13;19(3):173-180. doi: 10.1021/acscombsci.6b00178. Epub 2017 Jan 30.

Herein we report the polymer-supported synthesis of 3,4-dihydro-2H-1,4-oxazine-3-carboxylic acid derivatives using immobilized Fmoc-Ser(tBu)-OH and Fmoc-Thr(tBu)-OH as the starting materials. After the solid-phase-synthesis of N-alkyl-N-sulfonyl/acyl intermediates, the target dihydrooxazines were obtained using trifluoroacetic acid-mediated cleavage from the resin. This approach was also studied for the preparation of dihydrothiazines from immobilized Fmoc-Cys(Trt)-OH. Inclusion of triethylsilane in the cleavage cocktail resulted in the stereoselective formation of the corresponding morpholine/thiomorpholine-3-carboxylic acids. Stereochemical studies revealed the specific configuration of the newly formed stereocenter and also the formation of stable N-acylmorpholine rotamers.

2. Synthesis of the very acid-sensitive Fmoc-Cys(Mmt)-OH and its application in solid-phase peptide synthesis

K Barlos, D Gatos, O Hatzi, N Koch, S Koutsogianni Int J Pept Protein Res. 1996 Mar;47(3):148-53. doi: 10.1111/j.1399-3011.1996.tb01338.x.

S-4-methoxytrityl cysteine was synthesized and converted into the corresponding Fmoc-Cys(Mmt)-OH by its reaction with Fmoc-OSu. As compared to the corresponding Fmoc-Cys(Trt)-OH, the S-Mmt-function was found to be considerably more acid labile. Quantitative S-Mmt-removal occurs selectively in the presence of groups of the tert butyl type and S-Trt by treatment with 0.5-1.0% TFA. The new derivative was successfully utilized in the SPPS of Tyr1-somatostatin on 2-chlorotrityl resin. In this synthesis groups of the Trt-type were exclusively used for amino acid side-chain protection. Quantitative cleavage from the resin and complete deprotection was performed by treatment with 3% TFA in DCM-TES (95:5) for 30 min at RT. We observed no reduction of tryptophan under these conditions.

3. Efficient Chemical Protein Synthesis using Fmoc-Masked N-Terminal Cysteine in Peptide Thioester Segments

Abhisek Kar, Jamsad Mannuthodikayil, Sameer Singh, Anamika Biswas, Puneet Dubey, Amit Das, Kalyaneswar Mandal Angew Chem Int Ed Engl. 2020 Aug 24;59(35):14796-14801. doi: 10.1002/anie.202000491. Epub 2020 May 26.

We report an operationally simple method to facilitate chemical protein synthesis by fully convergent and one-pot native chemical ligations utilizing the fluorenylmethyloxycarbonyl (Fmoc) moiety as an N-masking group of the N-terminal cysteine of the middle peptide thioester segment(s). The Fmoc group is stable to the harsh oxidative conditions frequently used to generate peptide thioesters from peptide hydrazide or o-aminoanilide. The ready availability of Fmoc-Cys(Trt)-OH, which is routinely used in Fmoc solid-phase peptide synthesis, where the Fmoc group is pre-installed on cysteine residue, minimizes additional steps required for the temporary protection of the N-terminal cysteinyl peptides. The Fmoc group is readily removed after ligation by short exposure (<7 min) to 20 % piperidine at pH 11 in aqueous conditions at room temperature. Subsequent native chemical ligation reactions can be performed in presence of piperidine in the same solution at pH 7.