42134-49-6 Usage
Description
(3-Trimethylsilyl-2-propynyl)triphenylphosphonium bromide is a complex organic compound that features a triphenylphosphonium cation with a 3-trimethylsilyl-2-propynyl group attached to it. (3-TRIMETHYLSILYL-2-PROPYNYL)TRIPHENYLPHOSPHONIUM BROMIDE is characterized by its unique structure, which includes a trimethylsilyl group, a propynyl chain, and a triphenylphosphonium moiety. The presence of these functional groups endows the compound with specific chemical properties and potential applications in various fields.
Uses
Used in Pharmaceutical Industry:
(3-Trimethylsilyl-2-propynyl)triphenylphosphonium bromide is used as a synthetic intermediate for the development of olefinic peptides. These peptides exhibit renin inhibitor activity, which is crucial in the treatment of hypertension and other cardiovascular diseases. (3-TRIMETHYLSILYL-2-PROPYNYL)TRIPHENYLPHOSPHONIUM BROMIDE plays a significant role in the synthesis of these bioactive peptides, as it contributes to their unique structural features that enable them to effectively inhibit renin enzymes.
Specifically, (3-Trimethylsilyl-2-propynyl)triphenylphosphonium bromide is used as a key component in the synthesis of olefinic peptides that have demonstrated renin inhibitor activity against both hog kidney renin and human amniotic renin. This makes the compound an important tool in the development of novel therapeutic agents for the treatment of hypertension and related conditions. By incorporating this compound into the synthesis process, researchers can create peptides with enhanced renin inhibitory properties, potentially leading to more effective treatments for patients suffering from cardiovascular diseases.
Check Digit Verification of cas no
The CAS Registry Mumber 42134-49-6 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 4,2,1,3 and 4 respectively; the second part has 2 digits, 4 and 9 respectively.
Calculate Digit Verification of CAS Registry Number 42134-49:
(7*4)+(6*2)+(5*1)+(4*3)+(3*4)+(2*4)+(1*9)=86
86 % 10 = 6
So 42134-49-6 is a valid CAS Registry Number.
InChI:InChI=1/C24H26PSi.BrH/c1-26(2,3)21-13-20-25(22-14-7-4-8-15-22,23-16-9-5-10-17-23)24-18-11-6-12-19-24;/h4-12,14-19H,20H2,1-3H3;1H/q+1;/p-1
42134-49-6Relevant articles and documents
Total Synthesis of the Antidiabetic (Type 2) Lipid Mediator Protectin DX/PDX
Sancéau, Jean-Yves,Maltais, René,Poirier, Donald,Marette, André
, p. 495 - 505 (2019/01/24)
The first total synthesis of a lipid mediator derived from natural ?-3-fatty acid docosahexaenoic acid (DHA), 10S,17S-diHDHA (also referred to as protectin DX/PDX), was achieved in a convergent route (29 steps). The two chiral hydroxyl groups at C-10 and
Synthesis of exo-3-ammo-7-azabicyclo[2.2.1]heptanes as a class of malarial aspartic protease inhibitors: Exploration of two binding pockets
Zuercher, Martina,Hof, Fraser,Barandun, Luzi,Schuetz, Andri,Schweizer, W. Bernd,Meyer, Solange,Bur, Daniel,Diederich, Francois
supporting information; experimental part, p. 1707 - 1719 (2009/08/09)
The increasing prevalence of drug-resisLant strains of malaria-causing Plasmodium parasites necessitates the development of therapeutic agents that inhibit new biochemical targets. We herein describe the design, synthesis, and in vitro evaluation of a class of inhibitors that target the malarial aspartic proteases known as the plasmepsins. The title compounds feature a 7-azanorbornane skeleton that bears an exo-amino function, which was designed to interact with the catalytic dyad of aspartic proteases while providing vectors for the attachment of binding elements that target the flap and S1/S3 binding pockets at. the enzyme active site. Their synthesis takes advantage of a solvent-free and highly diastereoselective conjugate addition of amines to bicyclic vinyl sulfones. Structural optimization based on a little-known conformational preference of aryl sulfones produced the most potent inhibitors of this new class. In vitro assays demonstrate that the title compounds are capable of potent (IC50 ≥ 1.0 nM) inhibition of plasmepsins, while remaining relatively weak inhibitors of the closely related human enzymes cathepsins D and E. The ideal occupation of the flap pocket is crucial for both potency and selectivity over the human proteases. Differently functionalized compounds were synthesized to gain new insights info the molecular recognition properties of this cavity. Wiley-VCH Verlag GmbH & Co. KGaA.
