Thioredoxin reductase peptide acetate corresponds to residues 53–67 in thioredoxin reductase (TrxR), used in thioredoxin reductase research.Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx

Thioredoxin reductase peptide corresponds to residues 53–67 in thioredoxin reductase (TrxR), used in thioredoxin reductase research.Mammalian thioredoxin reductase (TR) catalyzes the reduction of the redox-active disulfide bond of thioredoxin (Trx) and is

Thioredoxin reductase peptide TFA corresponds to residues 53-67 in thioredoxin reductase (TrxR), used in thioredoxin reductase research..

Glutathione can occur in reduced (GSH), oxidized (GSSG), or in mixed disulfide forms and is ubiquitous in multiple biological systems serving as the major thiol-disulfide redox buffer of the cell. GSSG is the oxidized form of GSH . It can be reduced back to GSH through the NADPH-dependent enzyme glutathione reductase. GSSG functions as a hydrogen acceptor in the enzymatic determination of NADP+ and NADPH and can be a proximal donor in S-glutathionylation post translational modifications. The ratio of reduced glutathione to oxidized glutathione within cells is often used as an indicator of oxidative stress, with higher concentrations of GSSG predicting increased oxidative stress.

Homoglutathione, a tripeptide essential in eukaryotes, plays multifaceted roles in cellular redox regulation and exhibits taste-modifying effects [1] [2].

Angiotensin II human TFA, a potent vasoconstrictor within the renin/angiotensin system, plays a pivotal role in human blood pressure regulation primarily through interactions with the G-protein-coupled receptors Angiotensin II type 1 receptor (AT1R) and Angiotensin II type 2 receptor (AT2R). It not only prompts sympathetic nervous stimulation, aldosterone biosynthesis, and renal effects but also fosters growth in vascular smooth muscle cells and boosts collagen type I and III synthesis in fibroblasts. This action results in the thickening of the vascular wall and myocardium, alongside fibrosis. Additionally, Angiotensin II human TFA triggers apoptosis and encourages capillary formation from endothelial cells through the LOX-1 dependent redox-sensitive pathway [1] [2] [3] [4].

Bivalirudin TFA, a synthetic 20-residue peptide, serves as a reversible inhibitor of thrombin. Its IC50 value highlights its target specificity in vitro, where, combined with Eptifibatide (8 mg/mL) at a low concentration (70 ng/mL), it significantly reduces platelet aggregation induced by thrombin (0.2 U/mL) by approximately 90% [1]. The compound demonstrates no effect on thrombin generation assay (TGA) parameters up to 10 μmol/L [2]. Additionally, it facilitates the binding of MPO to BAEC, leading to functional alterations such as increased NO consumption and enhanced MPO-mediated redox modifications [3]. In vivo studies reveal its efficacy in preventing the rise of antiheparin/PF4 antibody IgG levels in rats, with significant findings from the toxicokinetic assessment signaling its safety profile at tested doses, although higher doses resulted in fatalities [4][5]. In clinical trials, its antithrombotic effects were explored, comparing it with alternatives like Ticagrelor and Clopidogrel in a Phase 4 study.