30189-48-1

Usage

Uses

Used in Pharmaceutical Research:
TERT-BUTYL N-(1-BENZYL-2-HYDRAZINO-2-OXOETHYL)CARBAMATE is used as an intermediate in the synthesis of pharmaceuticals for its potential to contribute to the development of new drugs with unique mechanisms of action.
Used in Organic Synthesis:
In the field of organic synthesis, TERT-BUTYL N-(1-BENZYL-2-HYDRAZINO-2-OXOETHYL)CARBAMATE is used as a building block for the creation of complex organic molecules, taking advantage of its reactive functional groups and structural diversity.
Used in the Development of Biologically Active Compounds:
Due to its unique structural features, TERT-BUTYL N-(1-BENZYL-2-HYDRAZINO-2-OXOETHYL)CARBAMATE is utilized in the design and synthesis of biologically active compounds, which may have applications in various therapeutic areas.

InChI:InChI=1/C14H21N3O3/c1-14(2,3)20-13(19)16-11(12(18)17-15)9-10-7-5-4-6-8-10/h4-8,11H,9,15H2,1-3H3,(H,16,19)(H,17,18)

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 51987-73-6 (S)-2-tert-butoxycarbonylamino-3-phenyl-propionic acid methyl ester 
• 7803-57-8 hydrazine hydrate 
• 63-91-2 L-phenylalanine 
• 119153-87-6 (C₅H₉O₂)C₉H₉NO(O)(CO₂C₂H₅) 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 

Downstream Products

• 1258792-66-3 C₃₂H₃₆N₄O₆ 
• 1258792-65-2 C₃₂H₃₆N₄O₆ 
• 1173675-82-5 C₁₅H₁₉N₃O₃S 
• 1360471-02-8 C₂₉H₃₈N₄O₅S 
• 1356072-52-0 tert-butyl (1S)-1-benzyl-2-{(2E/Z)-2-[(5-nitro-2-furyl)-methylene]hydrazine}-2-oxoethylcarbamate 
• 872017-66-8 (S)-tert-butyl (2-phenyl-1-(3-phenyl-1H-1,2,4-triazol-5-yl)ethyl)carbamate 
• 1246168-74-0 Boc-Phe-NH-NH-CS-Val-OMe 
• 1051936-73-2 C₂₂H₂₈N₄O₃S 
• 1051936-76-5 C₂₁H₂₅N₅O₅S 
• 1051936-71-0 tert-butyl (S)-(1-oxo-3-phenyl-1-(2-(phenylcarbamothioyl)hydrazinyl)propan-2-yl)carbamate 
• 1051936-74-3 C₂₁H₂₅BrN₄O₃S 
• 1051936-77-6 C₂₄H₃₂N₄O₆S 
• 1051936-75-4 C₂₁H₂₅BrN₄O₃S 
• 133383-03-6 ethyl (N-tert-butoxycarbonyl-L-phenylalanyl)(2-azaglutaminyl)glycinate 

Relevant academic research and scientific papers

Synthesis, molecular modeling and functional evaluation of a GnRH antagonist

In the present study, a series of novel Trp-Pro-Val containing peptides were prepared via solid-phase synthesis, and their structures were cyclized by a disulfide bridge, or modified by adding heterocycles of pyrazine, pyroglutamic acid, and 1,3,4-oxadiaz

The solid state VCD of a novel N-acylhydrazone trifluoroacetate

A novel N-acylhydrazone with pharmaceutical importance was subject of structural and IR/VCD investigations in the solid state. In the crystal structure, dimers of anion-cation pairs are stabilized by H-bonding and ionic interactions. Some less common inte

Targeting RECQL5 Functions, by a Small Molecule, Selectively Kills Breast Cancer in Vitro and in Vivo

Clinical and preclinical data reveal that RECQL5 protein overexpression in breast cancer was strongly correlated with poor prognosis, survival, and therapeutic resistance. In the current investigation, we report design, synthesis, and specificity of a small molecule, 4a, which can preferentially kill RECQL5-expressing breast cancers but not RECQL5 knockout. Our stringent analysis showed that compound 4a specifically sensitizes RECQL5-expressing cancers, while it did not have any effect on other members of DNA RECQL-helicases. Integrated approaches of organic synthesis, biochemical, in silico molecular simulation, knockouts, functional mutation, and rescue experiments showed that 4a potently inhibits RECQL5-helicase activity and stabilizes RECQL5-RAD51 physical interaction, leading to impaired HRR and preferential killing of RECQL5-expressing breast cancer. Moreover, 4a treatment led to the efficient sensitization of cisplatin-resistant breast cancers but not normal mammary epithelial cells. Pharmacologically, compound 4a was orally effective in reducing the growth of RECQL5-expressing breast tumors (human xenograft) in NUDE-mice with no appreciable toxicity to the vital organs.

Amino Acid Functionalized Organotin Trichlorides and Their Tin Sulfide Clusters

We present a new synthesis of functionalized tin sulfide clusters via organotin trichlorides with boc-protected amino acids (RAAcSnCl3). In this work we used non-polar (alanine, valine, leucine, phenylalanine and methionine), polar/neutral (serine and tyrosine) and basic (histidine) amino acids. We obtained single crystals from a Boc-protected valine derivative of the originally used organotin trichloride R1SnCl3 [R1 = CMe2CH2C(O)Me] and determined its structure by means of X-ray diffraction. A subsequent reaction with sulfide sources led to a variety of respective cluster structures. By using either (Me3Si)2S or Na2S, the reaction product turns out to be the defect-heterocubane cluster [(RAAcSn)3S4Cl] or the “doppeldecker”-type cluster [(RAAcSn)4S6], respectively, according to 119Sn NMR spectroscopy.

Efficient synthesis of novel conjugated 1,3,4-oxadiazole-peptides

We were interested in the design and synthesis of novel bioisosteric analogues of leuprolide acetate containing the oxadiazole moiety at the C- or N-terminal of the peptide. An efficient approach for the synthesis of 2-amino-1,3,4-oxadiazoles through the reaction of hydrazide with ammonium thiocyanate and desulfurization reaction of the thiosemicarbazides using different coupling reagents was employed. These compounds are bioisosteres of the amide bond. Furthermore, the coupling of 2-amino-1,3,4-oxadiazoles at the C-terminal of leuprolide analogues was carried out, using a coupling reagent in the solution phase. On the other hand, the addition of a 2-amino-1,3,4-oxadiazole to the N-terminal of the peptide sequence was carried out through the reaction of the 2-amino-1,3,4-oxadiazole with succinic anhydride that led to the formation of a carboxylic acid moiety. Addition of the synthesized oxadiazole containing carboxylic acid to the peptide sequence was performed using a coupling reagent and on the surface of the resin. The synthesized peptides containing the oxadiazole moiety at the C- or N-terminal of the peptide sequence are peptidomimetics of leuprolide acetate. All of the synthesized peptides were purified using preparative HPLC and their structures were confirmed using HR-MS (ESI).

COMPOUNDS AS MODULATORS OF TIGIT SIGNALLING PATHWAY

The present invention relates to compound of formula (I) as therapeutic agents to modulate the TIGIT signalling pathway. The invention also encompasses the use of the compound of formula (I) or a stereoisomer thereof or a pharmaceutically acceptable salt thereof for the treatment of diseases or disorders mediated by TIGIT.

VISTA SIGNALING PATHWAY INHIBITORY COMPOUNDS USEFUL AS IMMUNOMODULATORS

The present invention relates to VISTA signaling pathway inhibitory compounds of formula (I) which are useful as immune modulators for the treatment of various disease conditions including various types of cancer. The invention also encompasses the use of

Fragment Linking and Optimization of Inhibitors of the Aspartic Protease Endothiapepsin: Fragment-Based Drug Design Facilitated by Dynamic Combinatorial Chemistry

Fragment-based drug design (FBDD) affords active compounds for biological targets. While there are numerous reports on FBDD by fragment growing/optimization, fragment linking has rarely been reported. Dynamic combinatorial chemistry (DCC) has become a powerful hit-identification strategy for biological targets. We report the synergistic combination of fragment linking and DCC to identify inhibitors of the aspartic protease endothiapepsin. Based on X-ray crystal structures of endothiapepsin in complex with fragments, we designed a library of bis-acylhydrazones and used DCC to identify potent inhibitors. The most potent inhibitor exhibits an IC50value of 54 nm, which represents a 240-fold improvement in potency compared to the parent hits. Subsequent X-ray crystallography validated the predicted binding mode, thus demonstrating the efficiency of the combination of fragment linking and DCC as a hit-identification strategy. This approach could be applied to a range of biological targets, and holds the potential to facilitate hit-to-lead optimization.

Phenylimidazoles as potent and selective inhibitors of coagulation factor XIa with in vivo antithrombotic activity

Novel inhibitors of FXIa containing an (S)-2-phenyl-1-(4-phenyl-1H-imidazol-2-yl)ethanamine core have been optimized to provide compound 16b, a potent, reversible inhibitor of FXIa (Ki = 0.3 nM) having in vivo antithrombotic efficacy in the rabbit AV-shunt thrombosis model (ID50 = 0.6 mg/kg + 1 mg kg-1 h-1). Initial analog selection was informed by molecular modeling using compounds 11a and 11h overlaid onto the X-ray crystal structure of tetrahydroquinoline 3 complexed to FXIa. Further optimization was achieved by specific modifications derived from careful analysis of the X-ray crystal structure of the FXIa/11h complex. Compound 16b was well tolerated and enabled extensive pharmacologic evaluation of the FXIa mechanism up to the ID90 for thrombus inhibition.

IAP ANTAGONISTS

There are disclosed compounds that modulate the activity of inhibitors of apoptosis (IAPs), pharmaceutical compositions containing said compounds and methods of treating proliferative disorders and disorders of dysregulated apoptosis, such as cancer, utilizing the compounds of the invention.