71128-82-0Relevant articles and documents
Synthesis of novel Se-substituted selenocysteine derivatives as potential kidney selective prodrugs of biologically active selenol compounds: Evaluation of kinetics of β-elimination reactions in rat renal cytosol
Andreadou,Menge,Commandeur,Worthington,Vermeulen
, p. 2040 - 2046 (1996)
Eighteen Se-substituted selenocysteine derivatives were synthesized as potential kidney selective prodrugs which can be activated by renal cysteine conjugate β-lyase to selenium-containing chemoprotectants or antitumor agents. Selenocysteine derivatives with aliphatic and benzylic Se- substituents were synthesized by reducing selenocystine to selenocysteine followed by a reaction with the corresponding alkyl and benzyl halogenides. Selenocysteine derivatives with aromatic Se-substituents were synthesized by reaction of β-chloroalanine with substituted phenylselenol compounds, which were formed by reducing substituted diphenyl diselenides by NaBH4. The enzyme kinetic parameters (apparent K(m) and V(max)) of the β-elimination reaction of the selenocysteine conjugates were studied in rat renal cytosol. The results suggest that Se-substituted L-selenocysteine conjugates are extremely good substrates for renal cysteine conjugate β-lyases as indicated by low apparent K(m) and high V(max) values. The benzyl-substituted Se- conjugates appeared to be better substrates than the phenyl- and alkyl- substituted Se-conjugates. Corresponding L-cysteine S-conjugates were too poor substrates to obtain proper enzyme kinetics. Recently, local activation of cysteine S-conjugates by renal cysteine conjugate β-lyases was proposed as a new strategy to target antitumor agents to the kidney. The present results show that Se-substituted selenocysteine conjugates may be more promising prodrugs because these compounds are much better substrates for β- lyase.
Expanding the Structural Diversity of Protein Building Blocks with Noncanonical Amino Acids Biosynthesized from Aromatic Thiols
Wang, Yong,Chen, Xiaoxu,Cai, Wenkang,Tan, Linzhi,Yu, Yutong,Han, Boyang,Li, Yuxuan,Xie, Yuanzhe,Su, Yeyu,Luo, Xiaozhou,Liu, Tao
supporting information, p. 10040 - 10048 (2021/03/26)
Incorporation of structurally novel noncanonical amino acids (ncAAs) into proteins is valuable for both scientific and biomedical applications. To expand the structural diversity of available ncAAs and to reduce the burden of chemically synthesizing them, we have developed a general and simple biosynthetic method for genetically encoding novel ncAAs into recombinant proteins by feeding cells with economical commercially available or synthetically accessible aromatic thiols. We demonstrate that nearly 50 ncAAs with a diverse array of structures can be biosynthesized from these simple small-molecule precursors by hijacking the cysteine biosynthetic enzymes, and the resulting ncAAs can subsequently be incorporated into proteins via an expanded genetic code. Moreover, we demonstrate that bioorthogonal reactive groups such as aromatic azides and aromatic ketones can be incorporated into green fluorescent protein or a therapeutic antibody with high yields, allowing for subsequent chemical conjugation.
ANTIBACTERIAL COMPOUNDS
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Page/Page column 28, (2018/10/19)
Novel compounds having antimicrobial activitiy, in particular against Pseudomonas aeruginosa, Burkholderia cepaciaand/or Clostridium difficile, and a pharmaceutical composition containing the novel compound.
Total synthesis and stereochemical assignment of baringolin
Just-Baringo, Xavier,Bruno, Paolo,Ottesen, Lars K.,Canedo, Librada M.,Albericio, Fernando,Alvarez, Mercedes
, p. 7818 - 7821 (2013/08/23)
The thiopeptide antibiotic baringolin has been synthesized, and its structure and stereochemistry have been confirmed. The use of a strategy based on palladium-catalyzed cross-couplings permitted a modular construction of this natural product. Copyright
Internally stabilized selenocysteine derivatives: Syntheses, 77Se NMR and biomimetic studies
Phadnis, Prasad P.,Mugesh
, p. 2476 - 2481 (2007/10/03)
Selenocystine ([Sec]2) and aryl-substituted selenocysteine (Sec) derivatives are synthesized, starting from commercially available amino acid L-serine. These compounds are characterized by a number of analytical techniques such as NMR (1H, 13C and 77Se) and TOF mass spectroscopy. This study reveals that the introduction of amino/imino substituents capable of interacting with selenium may stabilize the Sec derivatives. This study further suggests that the oxidation-elimination reactions in Sec derivatives could be used for the generation of biologically active selenols having internally stabilizing substituents. The Royal Society of Chemistry 2005.
Facile chemoselective synthesis of dehydroalanine-containing peptides.
Okeley,Zhu,van Der Donk
, p. 3603 - 3606 (2007/10/03)
Useful methodology is described for the synthesis of dehydroalanine residues (II) within peptides. The unnatural amino acid (Se)-phenylselenocysteine (I) can be incorporated into growing peptide chains via standard peptide synthesis procedures. Subsequent
