S-Trityl-L-cysteine
Need Assistance?
  • US & Canada:
    +
  • UK: +

S-Trityl-L-cysteine

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

S-Trityl-L-cysteine is a cell-permeable, potent and selective inhibitor of mitotic kinesin Eg5, a protein required for establishing and maintaining a bipolar spindle. S-Trityl-L-cysteine inhibits basal and microtubule-activated ATPase activity of Eg5 (IC50 = 1 mM and 140 nM, respectively). S-Trityl-L-cysteine was shown to induce mitotic arrest in HeLa cells with an IC50 of 700 nM.

Category
L-Amino Acids
Catalog number
BAT-008108
CAS number
2799-07-7
Molecular Formula
C22H21NO2S
Molecular Weight
363.47
S-Trityl-L-cysteine
IUPAC Name
(2R)-2-amino-3-tritylsulfanylpropanoic acid
Synonyms
S-(Triphenylmethyl)-L-cysteine
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.232 g/cm3
Melting Point
155-170 °C
Boiling Point
524.7°C at 760 mmHg
Storage
Store at 2-8 °C
Solubility
Soluble in DMSO
InChI
InChI=1S/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)/t20-/m0/s1
InChI Key
DLMYFMLKORXJPO-FQEVSTJZSA-N
Canonical SMILES
C1=CC=C(C=C1)C(C2=CC=CC=C2)(C3=CC=CC=C3)SCC(C(=O)O)N

S-Trityl-L-cysteine, a widely utilized chemical compound in bioscience research, exhibits specific inhibitory properties.

Cancer Research: Delving into the realms of cancer biology, S-Trityl-L-cysteine emerges as an indispensable inhibitor, honing in on mitotic kinesin Eg5. By precisely disrupting Eg5’s function, researchers unravel the intricacies of mitosis and uncover potential avenues for cancer therapies. This compound plays a pivotal role in dissecting the mechanisms driving cancer cell proliferation and evaluating anti-cancer compounds geared towards halting aberrant cell division.

Neuroscience Studies: Embark on a journey through the enigmatic world of neuroscience, where S-Trityl-L-cysteine acts as a catalyst for investigating neuronal cell cycle regulation and growth. Through targeted inhibition of Eg5, scientists probe the significance of mitosis in neural development and unravel the mysteries of neurodegeneration. This pioneering research opens doors to fresh insights into neurological disorders and propels the evolution of innovative treatment modalities.

Drug Development: Witness the transformative power of S-Trityl-L-cysteine as a trailblazing lead compound in the realm of targeted anti-cancer drug development. By scrutinizing its interactions with specific molecular targets, researchers craft derivatives with heightened efficacy and diminished side effects. This iterative process forms the cornerstone of propelling novel therapeutic agents through the intricate drug development pipeline.

Biochemistry Research: Embark on a voyage into the intricate landscape of biochemistry, where S-Trityl-L-cysteine serves as a beacon for unraveling protein-protein interactions and structural stability. Through selective inhibition of distinct proteins, scientists unveil their roles within cellular processes, shedding light on fundamental biological functions. This illuminative journey fuels the development of drugs tailored to target these intricate interactions, driving forward the frontier of biochemistry research and therapeutic innovation.

1.Investigations on the antiproliferative effects of amino acid antagonists targeting for aminoacyl-tRNA synthetases. Part II--The antileukemic effect.
Laske R;Schönenberger H;Holler E Arch Pharm (Weinheim). 1989 Dec;322(12):857-62.
Amino acid antagonists with proven or potential inhibitory activities on aminoacyl-tRNA synthetases were tested for their antiproliferative effect against the murine leukemic cell line P388D1. Micromolar concentrations of the compounds S-tritylcysteine (18), fenitropan and beta-chloroalanine gave strong growth inhibition. In the mouse only 18 was effective against leukemia P388 (T/C = 211%). The inhibitory effect on aminoacyl-tRNA synthetases and the antiproliferative action on P388D1 or P388 could not be correlated.
2.Optimized S-trityl-L-cysteine-based inhibitors of kinesin spindle protein with potent in vivo antitumor activity in lung cancer xenograft models.
Good JA;Wang F;Rath O;Kaan HY;Talapatra SK;Podgórski D;MacKay SP;Kozielski F J Med Chem. 2013 Mar 14;56(5):1878-93. doi: 10.1021/jm3014597. Epub 2013 Feb 27.
The mitotic kinesin Eg5 is critical for the assembly of the mitotic spindle and is a promising chemotherapy target. Previously, we identified S-trityl-L-cysteine as a selective inhibitor of Eg5 and developed triphenylbutanamine analogues with improved potency, favorable drug-like properties, but moderate in vivo activity. We report here their further optimization to produce extremely potent inhibitors of Eg5 (K(i)(app) < 10 nM) with broad-spectrum activity against cancer cell lines comparable to the Phase II drug candidates ispinesib and SB-743921. They have good oral bioavailability and pharmacokinetics and induced complete tumor regression in nude mice explanted with lung cancer patient xenografts. Furthermore, they display fewer liabilities with CYP-metabolizing enzymes and hERG compared with ispinesib and SB-743921, which is important given the likely application of Eg5 inhibitors in combination therapies. We present the case for this preclinical series to be investigated in single and combination chemotherapies, especially targeting hematological malignancies.
3.Integrity of the Pericentriolar Material Is Essential for Maintaining Centriole Association during M Phase.
Seo MY;Jang W;Rhee K PLoS One. 2015 Sep 25;10(9):e0138905. doi: 10.1371/journal.pone.0138905. eCollection 2015.
A procentriole is assembled next to the mother centriole during S phase and remains associated until M phase. After functioning as a spindle pole during mitosis, the mother centriole and procentriole are separated at the end of mitosis. A close association of the centriole pair is regarded as an intrinsic block to the centriole reduplication. Therefore, deregulation of this process may cause a problem in the centriole number control, resulting in increased genomic instability. Despite its importance for faithful centriole duplication, the mechanism of centriole separation is not fully understood yet. Here, we report that centriole pairs are prematurely separated in cells whose cell cycle is arrested at M phase by STLC. Dispersal of the pericentriolar material (PCM) was accompanied. This phenomenon was independent of the separase activity but needed the PLK1 activity. Nocodazole effectively inhibited centriole scattering in STLC-treated cells, possibly by reducing the microtubule pulling force around centrosomes. Inhibition of PLK1 also reduced the premature separation of centrioles and the PCM dispersal as well. These results revealed the importance of PCM integrity in centriole association.
Online Inquiry
Verification code
Inquiry Basket