191228-76-9

Upstream product

• 2969-81-5 Ethyl 4-bromobutyrate 
• 540-38-5 p-Iodophenol 

Downstream Products

• 1023744-14-0 ethyl 4-(4-trimethylsilylethynylphenoxy)butyrate 
• 1357504-62-1 4-(4-{4-[4-(3-ethoxycarbonylpropoxy)phenyl]-(E)-but-1-en-3-ynyl}phenoxy)butyric acid ethyl ester 
• 1151683-54-3 ethyl 4-(4-ethynylphenoxy)butanoate 
• 1269831-61-9 C₆₀H₅₇O₁₀P 
• 1269831-60-8 C₆₀H₅₇O₉PSe 
• 731847-94-2 4-(4-iodophenoxy)butanoic acid 

Relevant academic research and scientific papers

Cyclodextrin-Based [c2]Daisy Chain Rotaxane Insulating Two Diarylacetylene Cores

A [c2]daisy chain rotaxane with two diarylacetylene cores was efficiently synthesized in 53 % yield by capping a C2-symmetric pseudo[2]rotaxane composed of two diarylacetylene-substituted permethylated α-cyclodextrins (PM α-CDs) with aniline stoppers. The maximum absorption wavelength of the [c2]daisy chain rotaxane remained almost unchanged in various solvents, unlike that of the stoppered monomer, indicating that the two independent diarylacetylene cores were insulated from the external environment by the PM α-CDs. Furthermore, the [c2]daisy chain rotaxane exhibited fluorescence emission derived from both diarylacetylene monomers and the excimer, which implies that the [c2]daisy chain structure can undergo contraction and extension. This is the first demonstration of a system in which excimer formation between two π-conjugated molecules within an isolated space can be controlled by the unique motion of a [c2]daisy chain rotaxane.

Does targeting Arg98 of FimH lead to high affinity antagonists?

Bacterial resistance has become an important challenge in the treatment of urinary tract infections. The underlying resistance mechanisms can most likely be circumvented with an antiadhesive approach, antagonizing the lectin FimH located at the tip of fim

PROTEIN KINASE C AGONISTS

The present disclosure relates generally to certain diacylglycerol lactone compounds, pharmaceutical compositions comprising said compounds, and methods of making and using said compounds and pharmaceutical compositions. The compounds and compositions disclosed herein may be used for the treatment or prevention of diseases, disorders, or infections modifiable by protein kinase C (PKC) agonists, such as HIV.

Dimerization of terminal arylalkynes in aqueous medium by ruthenium and acid promoted (RAP) catalysis: Acetate-assisted (sp)C-(sp2)C bond formation

The hexamethylbenzene ruthenium(II) dimer [{RuCl(m-Cl)(h6-C 6Me6)}]2 (5 mol%), tested among a series of ruthenium(II) and ruthenium(IV) complexes, represents an efficient precatalyst source for the dimerization of terminal arylalkynes ArCΞ CH [Ar=C 6H5, 3,4,5-(OMe)3C6H2, 4-MeOC 6H6, 2-MeOC6H6, 4-MeC 6H6, 2,4,5-Me3C6H2, 4-BrC 6H6, 4-ClC6H6, 4-FC 6H6, 4-HC(=O)C6H6, 4-CH 2=CHC6H6, 3-NCC6H6, 4-O2NC6H6, 4-EtO2C-(CH2)3OC6H 6, 4-HO(CH2CH2O)3C6H 6, 3-HO(CH2CH2O)3-C 6H6] in acetic acid/water mixture (1:1, v/v). The reactions proceed for 24 h at room temperature under heterogeneous conditions and afford the dimeric enyne derivatives (E)-Ar-CH=CH-C-C-Ar in high yields and stereoselectivity. The preformed acetato complex [RuCl(h6-C 6Me6)(k2-OAc)] catalyzes the dimerization of phenylacetylene under analogous conditions, with rapid substrate conversion. The presence of cosolvents of acetic acid different from water reduces dramatically the efficiency and selectivity of the reaction. The aqueous medium facilitates the activation stage of the precatalyst by assisting the splitting of the ruthenium dimer. The addition or generation in situ of acetate salts results in shorter reactions times (0.5-3 h) and excellent yields, due to the rapid formation of active acetato complexes. Circumstantial evidence indicates that the p-bound alkyne molecule is activated by intramolecular proton abstraction. This is currently the most efficient, E-selective and wide-scope catalytic system for the alkyne dimerization reaction in protic aqueous media.

HYDROXAMID ACID DERIVATIVES AS HISTONE DEACETYLASE (HDAC) INHIBITORS

A compound having the following formula (I): wherein R?1? is N-containing heterocyclic ring optionally substituted with one or more suitable substituent(s), R?2? is hydroxyamino, R?3? is hydrogen or a suitable substituent, L?1? is -(CH?2#191)?n#191- (wherein n is an integer of 0 to 6) optionally substituted with one or more suitable substituent(s), wherein one or more methylene(s) may be replaced with suitable heteroatom(s), and L?2? is lower alkenylene, or a salt thereof. The compound is useful as a histone deacetylase inhibitor.

HDAC inhibitor

A compound having the following formula (I): wherein R1 is N-containing heterocyclic ring optionally substituted with one or more suitable substituent(s), R2 is hydroxyamino, R3 is hydrogen or a suitable substituent, L1 is —(CH2)n— (wherein n is an integer of 0 to 6) optionally substituted with one or more suitable substituent(s), wherein one or more methylene(s) may be replaced with suitable heteroatom(s), and L2 is lower alkenylene, or a salt thereof. The compound is useful as a histone deacetylase inhibitor.

Discovery of potent nonpeptide inhibitors of stromelysin using SAR by NMR

With the use of an NMR-based method, potent (IC50 25 nM) nonpeptide inhibitors of the matrix metalloproteinase stromelysin (MMP-3) were discovered. The method, called SAR by NMR (for structure-activity relationships by nuclear magnetic resonance), involves the identification, optimization, and linking of compounds that bind to proximal sites on a protein. Using this technique, two ligands that bind weakly to stromelysin (acetohydroxamic acid, K(D) = 17 mM; 3-(cyanomethyl)-4'-hydroxybiphenyl, K(D) = 0.02 mM) were identified. On the basis of NMR-derived structural information, the two fragments were connected to produce a 15 nM inhibitor of this enzyme. This compound was rapidly discovered (less than 6 months) and required only a minimal amount of chemical synthesis. These studies indicate that the SAR by NMR method can be effectively applied to enzymes to yield potent lead inhibitors-an important part of the drug discovery process.

Biphenyl hydroxamate inhibitors of matrix metalloproteinases

Compounds of formula STR1 or a pharmaceutically acceptable salt thereof inhibit matrix metalloproteinases and TNFα secretion and are useful in the treatment of inflammatory disease states. Also disclosed are matrix metalloproteinases and TNFα secretion inhibiting compositions and a method for inhibiting matrix metalloproteinases and TNFα secretion.