26932-45-6

Basic information

• Product Name: D-Selenocystine
• Synonyms: 3,3'-Diselenobis(D-alanine);3,3'-Diselenobis[(S)-2-aminopropanoic acid];D-Selenocystine;(S,S)-3,3‘-Diseleno-bis(2-aMinopropionic acid);JULROCUWKLNBSN-QWWZWVQMSA-N
• CAS NO: 26932-45-6
• Molecular Formula: C₆H₁₂N₂O₄Se₂
• Molecular Weight: 334.09048
• Product Categories: Seleno Amino Acid
• Mol File: 26932-45-6.mol
• Article Data: 18

Chemical Properties

• Boiling Point: 108.25°C (estimate)
• Flash Point: 279.3°C
• Appearance: /
• Density: g/cm³
• PKA: 1.69±0.10(Predicted)
• CAS DataBase Reference: D-Selenocystine(CAS DataBase Reference)
• NIST Chemistry Reference: D-Selenocystine(26932-45-6)
• EPA Substance Registry System: D-Selenocystine(26932-45-6)

Safety Data

• Hazardous Substances Data: 26932-45-6(Hazardous Substances Data)

Usage

Description

D-Selenocystine is a naturally occurring, rare amino acid that is structurally similar to the more common L-cysteine, but with selenium replacing sulfur in the side chain. It is an essential component in the synthesis of certain selenoproteins, which play crucial roles in various biological processes, including antioxidant defense and thyroid hormone metabolism.
Source:
D-Selenocystine can be found in some organisms, such as bacteria and archaea, and is also synthesized by certain eukaryotes. It is typically obtained through the hydrolysis of proteins containing selenoamino acids or through biosynthetic pathways in specific organisms.
Production Methods:
D-Selenocystine can be produced through various methods, including chemical synthesis, microbial fermentation, and enzymatic processes. The most common method involves the use of seleno-D,L-homocysteine as a precursor, which is then converted to D-selenocystine through enzymatic reactions.

Uses

Used in Bioluminescence Applications:
D-Selenocystine is used as a key reagent in the preparation of firefly L-Luciferin, a molecule responsible for bioluminescence emission. This application is particularly relevant in the fields of biochemistry and molecular biology, where bioluminescent assays are widely used for various research purposes, such as gene expression analysis, cell signaling, and drug discovery.
Used in Pharmaceutical Industry:
D-Selenocystine is used as a precursor in the synthesis of certain pharmaceutical compounds, particularly those involving selenoamino acids. These compounds have potential applications in the treatment of various diseases, including cancer, neurological disorders, and viral infections.
Used in Nutritional Supplements:
Due to its role in the synthesis of selenoproteins, D-Selenocystine is used as an ingredient in nutritional supplements designed to support overall health and well-being. These supplements may be particularly beneficial for individuals with selenium deficiencies or those at risk for selenium-related health issues.
Used in Research and Development:
D-Selenocystine is also used in research and development for the study of selenium biochemistry, selenoprotein function, and the development of new drugs and therapies targeting selenium-dependent pathways.

Upstream product

• 2575-73-7 Se-benzyl-L-selenocysteine 
• 2575-73-7 2-amino-3-benzylselanyl-propionic acid 
• 7664-41-7 ammonia 
• 51887-89-9 β-chloro-L-alanine hydrochloride 
• 195324-31-3 dimethyl 3,3'-diselanediyl-(2R,2'R)-bis(2-((tertbutoxycarbonyl)amino)propanoate) 
• 109276-78-0 L-dibenzyl N,N'-di(benzyloxycarbonyl)selenocystinate 
• 25248-96-8 O-acetyl-D-serine 
• 19794-48-0 (2R)-serine O-sulfate 
• 3981-36-0 3-chloro-DL-alanine 
• 56410-68-5 3-chloro-DL-alanine methyl ester 
• 3614-08-2 L-selenocysteine 
• 83-88-5 riboflavin 
• 1148111-64-1 C₃H₆NO₂Se^(1-) 
• 1242409-39-7 hemiselenocystine 

Downstream Products

• 27025-41-8 Oxidized glutathione 
• 188609-44-1 C₁₃H₂₂N₄O₈SSe 
• 3614-08-2 L-selenocysteine 
• 83-88-5 riboflavin 
• 27317-69-7 N-tert-butoxycarbonyl-L-alanyl-L-alanine 
• 1365284-51-0 Fmoc-Sec(Bzl)-OH 
• 1639843-33-6 bisN-Fmoc-L-selenocystine 
• 1582790-34-8 C₁₀H₁₀O₄SSe 
• 176300-66-6 selenocysteine 
• 146552-76-3 Se-(4-methoxybenzyl)-L-selenocysteine 
• 2575-73-7 Se-benzyl-L-selenocysteine 
• 40055-98-9 oxidized glutathione 

Relevant articles and documents

Studies on the reaction between reduced riboflavin and selenocystine

Selenocysteine (Sec) is a crucial component of mammalian thioredoxin reductase (TrxR) where it serves as a nucleophile for disulfide bond rupture in thioredoxin (Trx). Generation of the reduced state of Sec in TrxR requires consecutive two electron transfer steps, namely: (i) from NADPH to flavin adenine dinucleotide, (ii) from reduced flavin to the disulfide bond Cys59-S-S-Cys64, and finally (iii) from Cys59 and Cys64 to the selenosulfide bond Cys497-S-Se-Sec498. In this work, we studied the reaction between reduced riboflavin (RibH2) and selenocystine (Sec-Sec), an oxidized form of Sec. The interaction between RibH2 and Sec-Sec proceeded relatively slowly in comparison with its reverse reaction, that is, reduction of riboflavin (Rib) by Sec. The rate constant for the reaction between RibH2 and Sec-Sec was (7.9?±?0.1)?×?10?2?M?1 s?1 (pH 7.0, 25.0°C). The reaction between Rib and Sec proceeded via two steps, namely, a rapid reversible binding of Rib to Sec having a protonated selenol group to form a Sec-Rib complex, followed by nucleophilic attack of Sec-Rib by a second Sec molecule harboring a deprotonated selenol group. The equilibrium constant for the overall reduction process of Rib by Sec is (1.2?±?0.1)?×?106?M?1 (25.0°C). The finding that the interaction of RibH2 with oxidized selenol is reversible with its equilibrium favored toward the reverse reaction provides an additional explanation for the exceptional mechanism of the mammalian Trx/TrxR system involving transient reduction of a disulfide bond.

Selenazolidine: A selenium containing proline surrogate in peptide science

In the search for new peptide ligands containing selenium in their sequences, we investigated l-4-selenazolidine-carboxylic acid (selenazolidine, Sez) as a proline analog with the chalcogen atom in the γ-position of the ring. In contrast to proteinogenic selenocysteine (Sec) and selenomethionine (SeMet), the incorporation within a peptide sequence of such a non-natural amino acid has never been studied. There is thus a great interest in increasing the possibility of selenium insertion within peptides, especially for sequences that do not possess a sulfur containing amino acid (Cys or Met), by offering other selenated residues suitable for peptide synthesis protocols. Herein, we have evaluated selenazolidine in Boc/Bzl and Fmoc/tBu strategies through the synthesis of a model tripeptide, both in solution and on a solid support. Special attention was paid to the stability of the Sez residue in basic conditions. Thus, generic protocols have been optimized to synthesize Sez-containing peptides, through the use of an Fmoc-Xxx-Sez-OH dipeptide unit. As an example, a new analog of the vasopressin receptor-1A antagonist was prepared, in which Pro was replaced with Sez [3-(4-hydroxyphenyl)-propionyl-d-Tyr(Me)-Phe-Gln-Asn-Arg-Sez-Arg-NH2]. Both proline and such pseudo-proline containing peptides exhibited similar pharmacological properties and endopeptidase stabilities indicating that the presence of the selenium atom has minimal functional effects. Taking into account the straightforward handling of Sez as a dipeptide building block in a conventional Fmoc/tBu SPPS strategy, this result suggested a wide range of potential uses of the Sez amino acid in peptide chemistry, for instance as a viable proline surrogate as well as a selenium probe, complementary to Sec and SeMet, for NMR and mass spectrometry analytical purposes.

Diphosphoric acid compounds, and preparation method and application thereof

The invention discloses compounds disclosed as Formula II. In the Formula II, R is disclosed in the specification, wherein R1 is H, OH or halogen; R2 is disclosed in the specification, n1=0-10, n2=0-10, and n3=0-10; Ar is aryl, arylidene, R99-substituted aryl or R99-substituted arylidene; at least one of R3, R4, R5 and R6 is selenium or sulfur atom, and the rest is carbon or nitrogen atom; and R3, R4, R5 and R6 are connected through a single bond or double bond. As for old patients with osteoporosis, the compounds can keep the osteocyte bone formation and bone destroy at an ideal dynamic balance.