S-Trityl-L-cysteine amide
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S-Trityl-L-cysteine amide

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Category
L-Amino Acids
Catalog number
BAT-004203
CAS number
166737-85-5
Molecular Formula
C22H22N2OS
Molecular Weight
362.50
S-Trityl-L-cysteine amide
IUPAC Name
(2R)-2-amino-3-tritylsulfanylpropanamide
Synonyms
L-Cys(Trt)-NH2; (R)-2-Amino-3-(Tritylthio)Propanamide
Appearance
White to off-white powder
Purity
≥ 98% (HPLC)
Density
1.183 g/cm3
Boiling Point
531.7°C
Storage
Store at 2-8°C
InChI
InChI=1S/C22H22N2OS/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,(H2,24,25)/t20-/m0/s1
InChI Key
OHWBGKONMFYEKL-FQEVSTJZSA-N
Canonical SMILES
C1=CC=C(C=C1)C(C2=CC=CC=C2)(C3=CC=CC=C3)SCC(C(=O)N)N

S-Trityl-L-cysteine amide, a chemical compound renowned for its ability to inhibit specific enzymes and proteins, finds widespread use in research. Here are four key applications of S-Trityl-L-cysteine amide:

Cancer Research: Positioned at the forefront of scientific exploration, S-Trityl-L-cysteine amide emerges as a potent inhibitor of Eg5, a pivotal enzyme essential for orchestrating mitotic spindle assembly during cell division. Researchers harness this compound to delve into the repercussions of Eg5 suppression on cancer cell proliferation and survival. This endeavor holds promise in identifying novel therapeutic avenues aimed at disrupting spindle assembly in the realm of cancer treatment.

Cell Cycle Studies: Delving into the intricacies of the cell cycle, S-Trityl-L-cysteine amide emerges as a valuable tool for dissecting the mechanics of mitosis, particularly through its inhibition of Eg5. Scientists can scrutinize the repercussions of Eg5 blockade on chromosome alignment, segregation, and the overarching progress of mitosis. This detailed examination sheds light on the fundamental processes governing cell division and unveils potential nodes for therapeutic intervention.

Anticancer Drug Development: Fueled by its unique mechanism of action targeting the mitotic machinery, S-Trityl-L-cysteine amide assumes a pivotal role as a lead compound in the quest for novel anticancer agents. By fine-tuning its structural composition, researchers endeavor to heighten its potency and specificity against cancerous cells. This chemical framework stands poised to catalyze the innovation of cutting-edge anticancer medications with minimized side effects.

Pharmacological Research: Extending beyond oncology, S-Trityl-L-cysteine amide serves as a linchpin in diverse pharmacological inquiries seeking to unravel its broader biological impacts. Scientists meticulously explore its interactions with a myriad of cellular proteins and pathways to unveil untapped therapeutic potentials. This holistic investigation broadens the horizons of S-Trityl-L-cysteine amide’s clinical applicability, paving the way for enhanced therapeutic efficacy across diverse medical landscapes.

1. Various effects of two types of kinesin-5 inhibitors on mitosis and cell proliferation
Jun-Ichi Sawada, Kenji Matsuno, Naohisa Ogo, Akira Asai Biochem Pharmacol. 2021 Nov;193:114789. doi: 10.1016/j.bcp.2021.114789. Epub 2021 Sep 25.
Kinesin-5 has received considerable attention as a new target for mitosis. Various small-molecule compounds targeting kinesin-5 have been developed in the last few decades. However, the differences in the cellular effects of kinesin-5 inhibitors remain poorly understood. Here, we used two different kinesin-5 inhibitors, biphenyl-type PVZB1194 and S-trityl-L-cysteine-type PVEI0021, to examine their effects on molecular events involving kinesin-5. Our biochemical study of kinesin-5 protein-protein interactions showed that PVZB1194-treated kinesin-5 interacted with TPX2 microtubule nucleation factor, Aurora-A kinase, receptor for hyaluronan-mediated motility, and γ-tubulin, as did untreated mitotic kinesin-5. However, PVEI0021 prevented kinesin-5 from binding to these proteins. In mitotic HeLa cells recovered from nocodazole inhibition, kinesin-5 colocalized with these binding proteins, along with microtubules nucleated near kinetochores. By acting on kinesin-5 interactions with chromatin-associated microtubules, PVZB1194, rather than PVEI0021, not only affected the formation of dispersed microtubule clusters but also enhanced the stability of microtubules. In addition, screening for mitotic inhibitors working synergistically with the kinesin-5 inhibitors revealed that paclitaxel synergistically inhibited HeLa cell proliferation only with PVZB1194. In contrast, the Aurora-A inhibitor MLN8237 exerted a synergistic anti-cell proliferation effect when combined with either inhibitor. Together, these results have provided a better understanding of the molecular action of kinesin-5 inhibitors and indicate their usefulness as molecular tools for the study of mitosis and the development of anticancer agents.
2. Optimized S-trityl-L-cysteine-based inhibitors of kinesin spindle protein with potent in vivo antitumor activity in lung cancer xenograft models
James A D Good, Fang Wang, Oliver Rath, Hung Yi Kristal Kaan, Sandeep K Talapatra, Dawid Podgórski, Simon P MacKay, Frank Kozielski 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. A 'conovenomic' analysis of the milked venom from the mollusk-hunting cone snail Conus textile--the pharmacological importance of post-translational modifications
Zachary L Bergeron, et al. Peptides. 2013 Nov;49:145-58. doi: 10.1016/j.peptides.2013.09.004. Epub 2013 Sep 18.
Cone snail venoms provide a largely untapped source of novel peptide drug leads. To enhance the discovery phase, a detailed comparative proteomic analysis was undertaken on milked venom from the mollusk-hunting cone snail, Conus textile, from three different geographic locations (Hawai'i, American Samoa and Australia's Great Barrier Reef). A novel milked venom conopeptide rich in post-translational modifications was discovered, characterized and named α-conotoxin TxIC. We assign this conopeptide to the 4/7 α-conotoxin family based on the peptide's sequence homology and cDNA pre-propeptide alignment. Pharmacologically, α-conotoxin TxIC demonstrates minimal activity on human acetylcholine receptor models (100 μM, <5% inhibition), compared to its high paralytic potency in invertebrates, PD50 = 34.2 nMol kg(-1). The non-post-translationally modified form, [Pro](2,8)[Glu](16)α-conotoxin TxIC, demonstrates differential selectivity for the α3β2 isoform of the nicotinic acetylcholine receptor with maximal inhibition of 96% and an observed IC50 of 5.4 ± 0.5 μM. Interestingly its comparative PD50 (3.6 μMol kg(-1)) in invertebrates was ~100 fold more than that of the native peptide. Differentiating α-conotoxin TxIC from other α-conotoxins is the high degree of post-translational modification (44% of residues). This includes the incorporation of γ-carboxyglutamic acid, two moieties of 4-trans hydroxyproline, two disulfide bond linkages, and C-terminal amidation. These findings expand upon the known chemical diversity of α-conotoxins and illustrate a potential driver of toxin phyla-selectivity within Conus.
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