2799-07-7

Basic information

• Product Name: S-Trityl-L-cysteine
• Synonyms: 3-(tritylthio)-l-alanin;3-tritylthio-l-alanine;s-(triphenylmethyl)-l-cystein;H-CYS(TRT)-OH;CYSTEINE(TRT)-OH;EG5 INHIBITOR II;NSC 83265;S-(TRIPHENYLMETHYL)-L-CYSTEINE
• CAS NO: 2799-07-7
• Molecular Formula: C₂₂H₂₁NO₂S
• Molecular Weight: 363.47
• EINECS: 218-195-8
• Product Categories: Amino Acids Derivatives;Cysteine [Cys, C];Amino Acids and Derivatives;Amino Acids 13C, 2H, 15N;Amino Acid Derivatives;Amino Acids & Derivatives;Aromatics;Chiral Reagents;Enzyme substrates;Cell Cycle Regulation
• Mol File: 2799-07-7.mol
• Article Data: 24

Chemical Properties

• Melting Point: 182-183 °C (dec.)(lit.)
• Boiling Point: 524.7 °C at 760 mmHg
• Flash Point: 271.2 °C
• Appearance: almost white to light yellow granular powder
• Density: 1.1342 (rough estimate)
• Vapor Pressure: 7.71E-12mmHg at 25°C
• Refractive Index: 111 ° (C=0.8, 0.04mol Ethanolic HCl)
• Storage Temp.: -20°C
• Solubility: Soluble in DMSO (up to 20 mg/ml).
• PKA: 2.22±0.10(Predicted)
• Stability: Stable for 2 years from date of purchase as supplied. Solutions in DMSO may be stored at -20°C for up to 1 week.
• BRN: 2339626
• CAS DataBase Reference: S-Trityl-L-cysteine(CAS DataBase Reference)
• NIST Chemistry Reference: S-Trityl-L-cysteine(2799-07-7)
• EPA Substance Registry System: S-Trityl-L-cysteine(2799-07-7)

Safety Data

• Hazard Codes: Xn
• Statements: 22
• Safety Statements: 22-24/25
• WGK Germany: 3
• RTECS: AY7710000
• Hazardous Substances Data: 2799-07-7(Hazardous Substances Data)

Usage

Description

S-Trityl-L-cysteine (STLC), with the chemical formula C20H19NO2S, is a non-natural, sulfur-containing amino acid that serves as a protected cysteine for peptide synthesis. It is a cell-permeable inhibitor of the mitotic kinesin Eg5, which plays a crucial role in preventing mitotic progression. STLC has demonstrated antitumor activity, as evidenced by its performance in the NCI 60 tumor cell line screen, with a mean growth concentration (GI50) of 1.31 μM for a panel of 60 different tumor cell lines. It is characterized by its almost white to light yellow granular powder appearance.

Uses

Used in Pharmaceutical Industry:
S-Trityl-L-cysteine is used as a protected cysteine for peptide synthesis, which is essential in the development of various pharmaceutical compounds. Its role in inhibiting the mitotic kinesin Eg5 makes it a potential candidate for the development of anti-cancer drugs, as it can prevent mitotic progression and exhibit antitumor activity.
Used in Chemical Synthesis:
S-Trityl-L-cysteine is used as a reagent in solution phase peptide synthesis (SPPS), where it aids in the formation of peptide bonds and contributes to the synthesis of complex peptide structures.
Used in Cation-Sensing Applications:
S-Trityl-L-cysteine is used as a metal-binding agent to synthesize substituted ferrocenoyl peptide conjugates using HBTU peptide coupling reagent. This application is particularly relevant in the development of cation-sensing solutions, where peptide-metal interactions are crucial for detecting and analyzing the presence of specific metal ions.

Biological Activity

Potent, cell-permeable, selective inhibitor of mitotic kinesin Eg5, a protein required for establishing and maintaining a bipolar spindle. Inhibits basal ATPase activity (IC 50 = 1 mM) and microtubule-activated ATPase activity of Eg5 (IC 50 = 140 nM). Induces mitotic arrest in HeLa cells with an IC 50 of 700 nM. Displays antitumor activity.

References

1) DeBonis et al. (2004) In vitro screening for inhibitors of the human mitotic kinesin Eg5 with antimitotic and antitumour activities; Mol. Cancer Ther. 3 1079 2) Brier et al. (2004) Identification of the protein binding region of S-trityl-L-cysteine, a new potent inhibitor of mitotic kinesin Eg5; Biochemistry 43 13072 3) Skoufias et al. (2006) S-trityl-l-cysteine is a reversible, tight-binding inhibitor of the human kinesin eg5 that specifically blocks mitotic progression; J. Biol. Chem., 281 17559

InChI:InChI=1/C22H21NO2S/c23-20(21(24)25)16-26-22(17-10-4-1-5-11-17,18-12-6-2-7-13-18)19-14-8-3-9-15-19/h1-15,20H,16,23H2,(H,24,25)

Upstream product

• 76-84-6 triphenylmethyl alcohol 
• 52-89-1 l-cysteine hydrochloride 
• 76-83-5 trityl chloride 
• 103213-32-7 N-(9-fluorenylmethoxycarbonyl)-S-trityl-L-cysteine 
• 93-58-3 benzoic acid methyl ester 
• 100-59-4 phenylmagnesium chloride 
• 591-51-5 phenyllithium 
• 32443-99-5 D-cysteine hydrochloride 
• 52-90-4 L-Cysteine 
• 880762-43-6 trifluoromethanesulfonic acid (R)-2,2,2-trifluoro-1-(4-fluorophenyl)ethyl ester 
• 921-01-7 D-cysteine 

Downstream Products

• 21947-98-8 N-tert-butyloxycarbonyl-S-trityl-L-cysteine 
• 96865-72-4 (R)-2-allyloxycarbonylamino-3-tritylthio-propionic acid 
• 96845-11-3 (R)-N-2,2,2-trichloroethoxycarbonyl-(S-trityl)cysteine 
• 76587-61-6 S-(triphenylmethyl)-L-cysteine tert-butyl ester 
• 166169-98-8 N-methyl-Cys(Trt) 
• 948586-45-6 N^α-nosyl-S-trityl-L-cysteine 
• 26988-59-0 N-Boc-S-trityl-L-cysteine dicyclohexylamine salt 
• 1159989-15-7 C₄₀H₃₆N₂O₆S 

Relevant articles and documents

Palladium Mediated Rapid Deprotection of N-Terminal Cysteine under Native Chemical Ligation Conditions for the Efficient Preparation of Synthetically Challenging Proteins

Facilitating the process of chemical protein synthesis is an important goal in order to enable the efficient preparation of large and novel protein analogues. Native chemical ligation, which is widely used in the synthesis and semisynthesis of proteins, has been going through several developments to expedite the synthetic process and to obtain the target protein in high yield. A key aspect of this approach is the utilization of protecting groups for the N-terminal Cys in the middle fragments, which bear simultaneously the two reactive groups, i.e., N-terminal Cys and C-terminal thioester. Despite important progress in this area, as has been demonstrated in the use of thiazolidine protecting group in the synthesis of over 100 proteins, finding optimal protecting group(s) remains a challenge. For example, the thiazolidine removal step is very slow (>8 h), and in some cases the applied conditions lead to undesired side reactions. Here we show that water-soluble palladium(II) complexes are excellent reagents for the effective unmasking of thiazolidine, enabling its complete removal within 15 min under native chemical ligation conditions. Moreover, palladium is also able to rapidly remove propargyloxycarbonyl-protecting group from the N-terminal Cys in a similar efficiency. The utility of the new removal conditions for both protecting groups is exemplified in the rapid and efficient synthesis of Lys34-ubiquitinated H2B and for the first time neddlyated peptides derived from cullin1. The current approach expands the use of palladium in protein chemistry and should significantly facilitate the chemical and semisynthesis of synthetically challenging proteins from multiple fragments.

3-Mercaptopropionic acid-mediated synthesis of peptide and protein thioesters

Peptides and proteins fragment sequence-specifically in the presence of 3-mercaptopropionic acid to afford thioesters which can be used in native chemical ligation reactions. The Royal Society of Chemistry.

Expeditious and practical synthesis of tertiary alcohols from esters enabled by highly polarized organometallic compounds under aerobic conditions in Deep Eutectic Solvents or bulk water

An efficient protocol was developed for the synthesis of tertiary alcohols via nucleophilic addition of organometallic compounds of s-block elements (Grignard and organolithium reagents) to esters performed in the biodegradable choline chloride/urea eutectic mixture or in water. This approach displays a broad substrate scope, with the addition reaction proceeding quickly (20 s reaction time) and cleanly, at ambient temperature and under air, straightforwardly furnishing the expected tertiary alcohols in yields of up to 98%. The practicability of the method is exemplified by the sustainable synthesis of some representative S-trityl-L-cysteine derivatives, which are a potent class of Eg5 inhibitors, also via telescoped one-pot processes.

Convergent Total Synthesis of the Siderophore Piscibactin as Its Ga3+Complex

The siderophore piscibactin is a key virulence factor involved in the iron uptake of pathogenic bacteria Photobacterium damselae subsp. piscicida and Vibrio anguillarum, responsible for the fish diseases photobacterioisis (pasteurellosis) and vibriosis, respectively. A convergent total synthesis of its Ga3+ complex using l-/d-cysteine as chiral agents and Meldrum's acid is described. A Staudinger reduction/Aza-Wittig process in the synthesis of the acid-sensitive β-hydroxy-2,4-disubstituted thiazoline moiety and the convenient protecting groups was a key step in this synthesis.