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Fmoc-D-cysteine

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

Fmoc-D-cysteine is an N-Fmoc-protected form of D-Cysteine. D-Cysteine is a strong inhibitor of Escherichia coli growth and also functions to provide inorganic sulfates for the sulfation of xenobiotics. D-Cysteine is a non-physiological isomer of L-Cysteine, and is not involved in protein or glutathione synthesis.

Category

Fmoc-Amino Acids

Catalog number

BAT-007662

CAS number

157355-80-1

Molecular Formula

C18H17NO4S

Molecular Weight

343.40

IUPAC Name

2-(9H-fluoren-9-ylmethoxycarbonylamino)-3-sulfanylpropanoic acid

Synonyms

N-[(9H-Fluoren-9-ylmethoxy)carbonyl]-L-cysteine; Fmoc-L-Cys-OH; Fmoc-cysteine; N-(9-Fluorenylmethoxycarbonyl)cysteine

Related CAS

135248-89-4 (R-isomer)

Appearance

White Solid

Purity

96%

Density

1.337±0.06 g/cm3(Predicted)

Melting Point

>100°C(dec.)

Boiling Point

574.4±50.0 °C(Predicted)

Storage

Store at -20°C Under inert atmosphere

Solubility

soluble in DMF, DMSO, Methanol

InChI

InChI=1S/C18H17NO4S/c20-17(21)16(10-24)19-18(22)23-9-15-13-7-3-1-5-11(13)12-6-2-4-8-14(12)15/h1-8,15-16,24H,9-10H2,(H,19,22)(H,20,21)

InChI Key

RMTDKXQYAKLQKF-UHFFFAOYSA-N

Canonical SMILES

C1=CC=C2C(=C1)C(C3=CC=CC=C32)COC(=O)NC(CS)C(=O)O

Fmoc-D-cysteine, a derivative of cysteine often utilized in peptide synthesis and diverse biochemical applications, holds significant value. Here are four key applications of Fmoc-D-cysteine:

Peptide Synthesis: Serving as a crucial component in peptide and protein synthesis, Fmoc-D-cysteine enables the integration of D-cysteine, imparting distinctive structural and functional characteristics to peptides. This plays a pivotal role in crafting peptide-based drugs and exploring the intricate relationships between peptide structures and activities.

Protein Engineering: Within the realm of protein engineering, Fmoc-D-cysteine plays a pivotal role in introducing thiol groups into peptides, facilitating the formation of disulfide bonds. These bonds are instrumental in stabilizing the three-dimensional configuration of proteins and peptides, aiding in the investigation of protein folding, stability, and functionality.

Bioconjugation: Enabling bioconjugation techniques, Fmoc-D-cysteine acts as a reactive site for attaching various molecules like fluorescent dyes or bioactive compounds to peptides. This enhances the detection, visualization, and targeting capabilities of peptides in research and therapeutic settings. Its utilization ensures precise site-specific attachment, enhancing control over the conjugation process.

Chirality Studies: In the exploration of chirality and enantiomeric effects in biochemical processes, Fmoc-D-cysteine plays an indispensable role. By utilizing the D-isomer of cysteine, researchers can delve into the distinct functions and biological activities of L- and D-amino acids in nature. This contributes to a deeper comprehension of stereochemistry in biological systems, informing strategies for drug design and development.

1. Selenopeptide chemistry

Markus Muttenthaler, Paul F Alewood J Pept Sci. 2008 Dec;14(12):1223-39. doi: 10.1002/psc.1075.

This review focuses on the chemical aspects of the 21st proteinogenic amino acid, selenocysteine in peptides and proteins. It describes the physicochemical properties of selenium/sulfur and selenocysteine/cysteine based on comprehensive structural (X-ray, NMR, CD) and biological data, and illustrates why selenocysteine is considered the most conservative substitution of cysteine. The main focus lies on the synthetic methods on selenocysteine incorporation into peptides and proteins, including an overview of the selenocysteine building block syntheses for Boc- and Fmoc-SPPS. Selenocysteine-mediated reactions such as native chemical ligation and dehydroalanine formation are addressed towards peptide conjugation. Selenopeptides have very interesting and distinct properties which lead to a diverse range of applications such as structural, functional and mechanistic probes, robust scaffolds, enzymatic reaction design, peptide conjugations and folding tools.

2. Rethinking Cysteine Protective Groups: S-Alkylsulfonyl-l-Cysteines for Chemoselective Disulfide Formation

Olga Schäfer, David Huesmann, Christian Muhl, Matthias Barz Chemistry. 2016 Dec 12;22(50):18085-18091. doi: 10.1002/chem.201604391. Epub 2016 Oct 31.

The ability to reversibly cross-link proteins and peptides grants the amino acid cysteine its unique role in nature as well as in peptide chemistry. We report a novel class of S-alkylsulfonyl-l-cysteines and N-carboxy anhydrides (NCA) thereof for peptide synthesis. The S-alkylsulfonyl group is stable against amines and thus enables its use under Fmoc chemistry conditions and the controlled polymerization of the corresponding NCAs yielding well-defined homo- as well as block co-polymers. Yet, thiols react immediately with the S-alkylsulfonyl group forming asymmetric disulfides. Therefore, we introduce the first reactive cysteine derivative for efficient and chemoselective disulfide formation in synthetic polypeptides, thus bypassing additional protective group cleavage steps.

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.