223611-40-3

Upstream product

• 76-83-5 trityl chloride 
• 77544-60-6 p-toluenesulfonic acid 2-[2-[2-(2-hydroxyethoxy)ethoxy]ethoxy]ethyl ester 
• 112-60-7 Tetraethylene glycol 
• 98-59-9 p-toluenesulfonyl chloride 
• 125274-16-0 1,1,1-triphenyl-2,5,8,11-tetraoxatridecan-13-ol 

Downstream Products

• 223611-41-4 1-O-trityl-11-thioacetyl-3,6,9-trioxa-undecanol 
• 1107609-32-4 tetraethylene glycol trityl-6-cyano-2-naphthyl ether 
• 1201411-02-0 C₃₂H₃₆N₆O₄ 
• 477775-73-8 1-phenyl-2,5,8,11,14,17,20,23-octaoxapenta-cosan-25-ol 
• 1351556-81-4 2-(2-{2-[2-(2-{2-[2-(2-prop-2-ynyloxyethoxy)ethoxy]ethoxy}ethoxy)ethoxy]ethoxy}ethoxy)ethanol 
• 1036204-61-1 C₂₇H₅₂O₁₃ 
• 1351556-80-3 1,1,1-triphenyl-2,5,8,11,14,17,20,23,26-nonaoxanonacos-28-yne 
• 1585235-92-2 63-(4-(3,3,4,4,5,5,6,6,7,7,8,8,9,9,10,10,10-heptadecafluorodecyl)phenyl)-1,1,1-triphenyl-2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50,53,56,59,62-henicosaoxatrihexacontane 
• 1585235-90-0 51-(4-(3,3,4,4,5,5,6,6,7,7,8,8,9,9,10,10,10-heptadecafluorodecyl)phenyl)-1,1,1-triphenyl-2,5,8,11,14,17,20,23,26,29,32,35,38,41,44,47,50-heptadecaoxahenpentacontane 
• 1585235-88-6 9-(4-(3,3,4,4,5,5,6,6,7,7,8,8,9,9,10,10,10-heptadecafluorodecyl)phenyl)-1,1,1-triphenyl-2,5,8,11,14,17,20,23,26,29,32,35,38-tridecaoxanonatriacontane 
• 1585235-86-4 27-(4-(3,3,4,4,5,5,6,6,7,7,8,8,9,9,10,10,10-heptadecafluorodecyl)phenyl)-1,1,1-triphenyl-2,5,8,11,14,17,20,23,26-nonaoxaheptacosane 
• 223611-36-7 thioacetic acid S-[2-(2-{2-[2-(2-{2-[2-(2-trityloxy-ethoxy)-ethoxy]-ethoxy}-ethylsulfanyl)-ethoxy]-ethoxy}-ethoxy)-ethyl] ester 
• 223611-44-7 methanesulfonic acid 2-(2-{2-[2-(2-{2-[2-(2-trityloxy-ethoxy)-ethoxy]-ethoxy}-ethylsulfanyl)-ethoxy]-ethoxy}-ethoxy)-ethyl ester 
• 223611-43-6 2-(2-{2-[2-(2-{2-[2-(2-trityloxy-ethoxy)-ethoxy]-ethoxy}-ethylsulfanyl)-ethoxy]-ethoxy}-ethoxy)-ethanol 

Relevant academic research and scientific papers

INHIBITORS OF CYCLIN-DEPENDENT KINASES AND USES THEREOF

Provided are novel compounds of Formula (I); pharmaceutically acceptable salts thereof, and pharmaceutical compositions thereof, which are useful in the treatment of diseases and disorders mediated by CDK such as cancer.

METHOD FOR SYNTHESIS OF PROTEIN AMPHIPHILES

The present invention discloses a novel cost effective method for synthesis of protein/peptide amphiphiles irrespective of functional and structural classification of proteins useful in designing a vaccine candidate from antigenic protein. The protein modification of the present invention is universal and hence any protein/peptide can be converted into amphiphilic proteins/peptides.

SUPRAMOLECULAR PROTEIN ASSEMBLIES WITH ADVANCED FUNCTIONS AND SYNTHESIS THEREOF

The present invention discloses stimuli-sensitive protein conjugate which can make supramolecular protein assemblies and methods for using the same. The present invention provides simple and rational process for construction of said stimuli-sensitive spherical protein assemblies through supramolecular chemical strategy.

Fluorous synthesis of mono-dispersed poly(ethylene glycols)

Mono-dispersed poly(ethylene glycols) (PEGs) are of great value in the development of biopharmaceuticals. However, tedious synthesis limits the availability of mono-dispersed PEGs. To address this issue, a fluorous synthesis of mono-dispersed PEGs, discretely PEGylated surfactants and 19F magnetic resonance imaging (MRI) agents has been developed. During the synthesis, both fluorous and normal phase silica gel-based solid-phase extractions were successfully employed to simplify the purifications. This synthesis provided an easy access to valuable mono-dispersed PEGs and related molecules for biomedical application on multi-gram scales.

Synthesis of gemini surfactants with twelve symmetric fluorine atoms and one singlet 19F MR signal as novel 19F MRI agents

A family of fluorinated gemini surfactants derived from perfluoropinacol has been synthesized as novel 19F magnetic resonance imaging ( 19F MRI) agents. These fluorinated surfactants with 12 symmetric fluorine atoms and one singlet

Dynamic light scattering evidence for a ligand-induced motion between the two domains of glucoamylase G1 of Aspergillus niger with heterobivalent substrate analogues

Heterobifunctional ligands that bind at the same time to the catalytic domain and to the starch-binding domain of glucoamylase induce a conformational change of the protein, as shown by dynamic light scattering. The ligands consist of acarbose and β-cyclo