157522-54-8

Basic information

• Product Name: 2-bromoethyl triphenylmethyl sulfide
• Synonyms: 2-bromoethyl triphenylmethyl sulfide
• CAS NO: 157522-54-8
• Molecular Weight: 383.352
• Mol File: 157522-54-8.mol

Chemical Properties

• CAS DataBase Reference: 2-bromoethyl triphenylmethyl sulfide(CAS DataBase Reference)
• NIST Chemistry Reference: 2-bromoethyl triphenylmethyl sulfide(157522-54-8)
• EPA Substance Registry System: 2-bromoethyl triphenylmethyl sulfide(157522-54-8)

Safety Data

• Hazardous Substances Data: 157522-54-8(Hazardous Substances Data)

Upstream product

• 3695-77-0 triphenylmethanethiol 
• 106-93-4 ethylene dibromide 
• 76-83-5 trityl chloride 

Downstream Products

• 908131-40-8 lithium ({1-[2-(tritylthio)ethyl]-1H-imidazol-2-yl}thio)acetate 
• 908131-39-5 lithium 1-[2-(tritylthio)ethyl]-1H-imidazole-2-carboxylate 
• 259822-63-4 methyl (2S)-2-amino-4-(tritylsulfanyl)butanoate 
• 69955-57-3 (2S)-2-amino-4-(tritylsulfanyl)butanoic acid 
• 259822-62-3 (2R,5S)-2-isopropyl-3,6-dimethoxy-5-[2-(tritylsulfanyl)ethyl]-2,5-dihydropyrazine 
• 188121-42-8 N-phenyl[2-(2-tritylsulfanylethoxy)phenoxy]acetamide 
• 188121-43-9 N-p-Tolyl-2-[2-(2-tritylsulfanyl-ethoxy)-phenoxy]-acetamide 

Relevant articles and documents

Design and Ribosomal Incorporation of Noncanonical Disulfide-Directing Motifs for the Development of Multicyclic Peptide Libraries

The engineering of naturally occurring disulfide-rich peptides (DRPs) has been significantly hampered by the difficulty of manipulating disulfide pairing. New DRPs that take advantage of fold-directing motifs and noncanonical thiol-bearing amino acids are easy-to-fold with expected disulfide connectivities, representing a new class of scaffolds for the development of peptide ligands and therapeutics. However, the limited diversity of the scaffolds and particularly the use of noncanonical amino acids [e.g., penicillamine (Pen)] that are difficult to be translated by ribosomes greatly hamper the further development and application of these DRPs. Here, we designed and synthesized noncanonical bisthiol motifs bearing sterically obstructed thiol groups analogous to the Pen thiol to direct the folding of peptides into specific bicyclic and tricyclic structures. These bisthiol motifs can be ribosomally incorporated into peptides through a commercially available PURE system integrated with genetic code reprograming, which enables, for the first time, the in vitro expression of bicyclic peptides with two noncanonical and orthogonal disulfide bonds. We further constructed a bicyclic peptide library encoded by mRNA, with which new bicyclic peptide ligands with nanomolar affinity to proteins were successfully selected. Therefore, this study provides a new, general, and robust method for discovering de novo DRPs with new structures and functions not derived from natural peptides, which would greatly benefit the field of peptide drug discovery.

Hydrogen evolution reaction mediated by an all-sulfur trinuclear nickel complex

We report the synthesis and the characterization of a trinuclear nickel complex. Solid state and solution studies using X-ray diffraction, NMR and UV-vis spectroscopy highlight the square planar geometries around the metal centers and an all-sulfur coordi

GLUCAGON-LIKE PEPTIDE 1 (GLP-1) RECEPTOR AGONISTS AND THEIR PHARMACOLOGICAL METHODS OF USE

This invention provides peptides with novel modifications that provide suitable derivatization sites to improve the pharmacokinetic properties of the peptides. These GLP-1 modified peptides function in vivo as agonists of the GLP-1 receptor. The peptides of the present invention provide a new therapy for patients with decreased endogenous insulin secretion, for example, type 2 diabetics.

GLUCOSE-DEPENDENT INSULINOTROPIC POLYPEPTIDE (GIP) RECEPTOR AGONISTS AND THEIR PHARMACOLOGICAL METHODS OF USE

This invention provides peptides with novel modifications that provide suitable derivatization sites to improve the pharmacokinetic properties of the peptides. These modified peptides function in vivo as agonists of the GIP receptor. The peptides of the present invention provide a new therapy for patients with decreased endogenous insulin secretion, for example, type 2 diabetics.

SELECTIVE NEUROPEPTIDE Y2 RECEPTOR AGONISTS

This invention provides peptides that act as selective NPY2 receptor agonists and may be used to reduce food intake. The invention includes a peptide selected from a specific group of derivatized NPY-related peptides, or functional equivalents thereof. The invention is also directed to a method of treating obesity or related diseases in a mammal comprising administering a therapeutically effective amount of the peptide to said mammal to reduce food intake and body weight.

NEUROPEPTIDE Y4 RECEPTOR AGONISTS

This invention provides peptides that act as selective NPY4 receptor agonists in vitro and are efficacious in vivo to reduce food intake. The invention is a peptide selected from a specific group of derivatized PP-related peptides, or functional equivalents thereof. The invention is also directed to a method of treating a metabolic disease in a mammal comprising administering a therapeutically effective amount of the peptides to said mammal to reduce food intake and body weight.

PITUITARY ADENYLATE CYCLASE ACTIVATING PEPTIDE (PACAP) RECEPTOR (VPAC2) AGONISTS AND THEIR PHARMACOLOGICAL METHODS OF USE

This invention provides peptides with novel modifications that provide suitable derivatization sites to improve the pharmacokinetic properties of the peptides. These modified peptides function in vivo as agonists of the VPAC2 receptor. The peptides of the present invention provide a new therapy for patients with decreased endogenous insulin secretion, for example, type 2 diabetics.

The first asymmetric syntheses of L-homocysteine and L-homocystine

Asymmetric syntheses of L-homocysteine 1 and L-homocystine 2 are described. Alkylation of the carbanion derived from Schollkopf reagent 3 and ensuing hydrolyses gave S-triphenylmethyl-L-homocysteine 6. Removal of the triphenylmethyl group gave L-homocysteine 1 and subsequent oxidation provided L-homocystine 2.

Design, synthesis and evaluation of substituted triarylnipecotic acid derivatives as GABA uptake inhibitors: Identification of a ligand with moderate affinity and selectivity for the cloned human GABA transporter GAT- 3

γ-Aminobutyric acid (GABA) is the major inhibitory neurotransmitter in the mammalian central nervous system. Molecular biology has revealed the presence of four high-affinity GABA transporters in the brain, GAT-1, GAT-2, GAT-3, and BGT-1, the latter transporting both GABA and the osmolyte Betaine. We have shown that known GABA uptake inhibitors such as SK and F 89976-A, CI- 966, and Tiagabine exhibit high affinity and selectivity for GAT-1. In the present paper we describe the design and synthesis of a novel series of triarylnipecotic acid derivatives for evaluation as GABA uptake inhibitors. The design lead for this series of compounds was the nonselective GABA uptake inhibitor EGYT-3886, [(-)-2-phenyl-2-[(dimethylamino)ethoxy]-(1R)-1,7,7- trimethylbicyclo[2.2.1]heptane]. From this series of compounds (S)-1-[2- [tris(4-methoxyphenyl)methoxy]ethyl]-3-piperidinecarboxylic acid, 4(S) was identified as a novel ligand with selectivity for GAT-3. 4(S) displayed an IC50 of 5 μM at GAT-3, 21 μM at GAT-2, >200 μM at GAT-1, and 140 μM at BGT-1. This compound will be an important tool for evaluating the role of GAT-3 in neural function.