37076-47-4

Upstream product

• 58352-78-6 ethyl 2-(trityloxy)acetate 
• 79-14-1 glycolic Acid 
• 76-83-5 trityl chloride 
• 96-35-5 glycolic acid methyl ester 

Downstream Products

• 58352-80-0 Trityloxy-acetic acid 8-hydroxy-9,10-dioxo-9,10-dihydro-anthracen-1-yl ester 
• 851181-05-0 3-p-tolyl-5-trityloxymethyl-[1,2,4]oxadiazole 
• 851181-07-2 3-(4-ethyl-phenyl)-5-trityloxymethyl-[1,2,4]oxadiazole 
• 1428847-72-6 (S)-3,5-dichloro-4-(2-(3-(cyclopropylmethoxy)-4-(difluoromethoxy)phenyl)-2-(2-(trityloxy)acetoxy)ethyl)pyridine 1-oxide 
• 1275616-91-5 ethyl (2-trityloxyacetylamino)acetate 
• 1275616-92-6 (2-trityloxyacetylamino)acetic acid 

Relevant academic research and scientific papers

Activation of lysine-specific demethylase 1 inhibitor peptide by redox-controlled cleavage of a traceless linker

We have previously employed cyclization of a linear peptide as a strategy to modulate peptide function and properties, but cleavage to regenerate the linear peptide left parts of the linker structure on the peptide, interfering with its activity. Here, we focused on cyclization of a linear peptide via a “traceless” disulfide-based linkage that would be cleaved and completely removed in a reducing environment, regenerating the original linear peptide without any linker-related structure. Thus, the linker would serve as a redox switch that would be activated in the intracellular environment. We applied this strategy to a lysine-specific demethylase 1 (LSD1) inhibitor peptide 1. The resulting cyclic peptide 2 exhibited approximately 20 times weaker LSD1-inhibitory activity than peptide 1. Upon addition of reducing reagent, the linker was completely removed to regenerate the linear peptide 1, with full restoration of the LSD1-inhibitory activity. In addition, the cyclic peptide was far less susceptible to proteolysis than the linear counterpart. Thus, this switch design not only enables control of functional activity, but also improves stability. This approach should be applicable to a wide range of peptides, and may be useful in the development of peptide pharmaceuticals.

RESVERATROL GLYCOLATE AND TARTRATE DERIVATIVES AND SYNTHETIC METHODS THEREFOR

The invention is in the field of resveratrol derivative compounds and compositions, and methods for synthesizing same.

Improved solid phase synthesis of peptide carboxyamidomethyl (Cam) esters for enzymatic segment condensation

Peptide C-terminal carboxyamidomethyl (Cam-)esters are pivotal building blocks for enzymatic segment condensation and their yield and purity are crucial for the overall efficiency of this strategy. Although a few methods for their preparation have been di

DERIVATIVES OF 1-PHENYL-2-PYRIDINYL ALKYL ALCOHOLS AS PHOSPHODIESTERASE INHIBITORS

The invention relates to inhibitors of the phosphodiesterase 4 (PDE4) enzyme. More particularly, the invention relates to compounds that are derivatives of 1-phenyl-2-pyridinyl alkyl alcohols, methods of preparing such compounds, compositions containing them and therapeutic use thereof.

DERIVATIVES OF 1-PHENYL-2-PYRIDINYL ALKYL ALCOHOLS AS PHOSPHODIESTERASE INHIBITORS

The invention relates to inhibitors of the phosphodiesterase 4 (PDE4) enzyme. More particularly, the invention relates to compounds that are derivatives of 1-phenyl-2-pyridinyl alkyl alcohols, methods of preparing such compounds, compositions containing them and therapeutic use thereof.

Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and α-hydroxy acid residue containing peptides

Amyloid deposits are formed as a result of uncontrolled aggregation of (poly)peptides or proteins. Today several diseases are known, for example Alzheimer's disease, Creutzfeldt-Jakob disease, mad cow disease, in which amyloid formation is involved. Amylo

Synthesis of 3′,5′-Dipeptidyl Oligonucleotides

Peptide-DNA hybrids are richly functionalized analogues of biomolecules that may have applications as hybridization probes and antisense agents with tunable binding and targeting properties. So far, synthetic efforts have mainly focused on hybrids bearing a single peptide chain, either at the 5′- or the 3′-terminus. Such singly modified analogues are vulnerable to nuclease attack at the unmodified terminus. Here we report a convenient and high-yielding solid-phase synthesis of 3′- and 5′-modified analogues of DNA with aminoacyl and peptidyl appendages at both termini. Using MALDI-TOF mass spectra of crude products as the criterion, serine, glycolic acid, hydroxylauric acid, and dimethyl hydroxypropionic acid were tested as 3′-linker residues. The latter, together with a direct amide link at the 5′-terminus, gave the highest yields of hybrids. The optimized procedure assembles hybrids on a controlled pore glass support bearing three consecutive ω-hydroxy lauric acid linkers. This support greatly reduces side reactions observed with conventional supports, probably due to its ability to increase steric accessibility during coupling ("swelling") and its rapid hydrolysis during deprotection with ammonium hydroxide. Dihybrids with aromatic, basic, and acidic amino acid residues were prepared, including H-Phe-Gly-TGCGCA-DP-Phe-OH, where DP denotes the dimethyl hydroxypropionic acid linker, whose structure was confirmed via mass spectrometry and one- and two-dimensional NMR. Further, a mixed coupling with seven Fmoc-protected amino acids was shown to produce a combinatorial library of dipeptidyl DNA hybrids.