608-16-2

Usage

Uses

(+)-Biotin Methyl Ester is an protected intermediate in the synthesis of Biotin (B389040).

InChI:InChI=1/C11H18N2O3S/c1-16-9(14)5-3-2-4-8-10-7(6-17-8)12-11(15)13-10/h7-8,10H,2-6H2,1H3,(H2,12,13,15)/t7-,8-,10-/m0/s1

Upstream product

• 67-56-1 methanol 
• 91853-90-6 biotin chloride 
• 58-85-5 biotin 
• 186581-53-3 diazomethane 
• 18107-18-1 diazomethyl-trimethyl-silane 
• 7647-01-0 hydrogenchloride 
• 449729-48-0 5-[(3aS,6aR)-1-Benzyl-2-oxo-hexahydro-thieno[3,4-d]imidazol-(4Z)-ylidene]-pentanoic acid methyl ester 
• 116615-95-3 5-[(3aR,6aS)-1-Benzyl-2-oxo-hexahydro-thieno[3,4-d]imidazol-(6E)-ylidene]-pentanenitrile 
• 116615-96-4 5-((3aR,6S,6aS)-1-Benzyl-2-oxo-hexahydro-thieno[3,4-d]imidazol-6-yl)-pentanenitrile 
• 116615-92-0 (4R,5R)-1-Benzyl-4-(5-chloro-pent-1-ynylsulfanylmethyl)-5-hydroxy-imidazolidin-2-one 
• 75-36-5 acetyl chloride 
• 149-73-5 trimethyl orthoformate 
• 412319-73-4 2-(4-methoxy-butyl)-tetrahydro-thiophene-3,4-dicarboxylic acid diethyl ester 
• 58522-80-8 2-oxo-2,3-dihydro-4-(δ-methoxycarbonylbutyl)-1H-thieno<3,4-d>imidazole 

Downstream Products

• 83541-80-4 <3aS-(3aα,4β,6aα)>-Hexahydro-2-oxo-3-(phenylmethyl)-1H-thieno<3,4-d>imidazole-4-pentanoic acid methyl ester 
• 151526-81-7 <3aS-(3aα,4β,6aα)>-Hexahydro-2-oxo-1-(phenylmethyl)-1H-thieno<3,4-d>imidazole-4-pentanoic acid methyl ester 
• 58-85-5 biotin 
• 111790-37-5 N-biotinyl-1,2-diaminoethane 
• 122224-39-9 1-N-(4,4'-dimethoxytrityl)-D(+)-biotinol 
• 122224-34-4 (1-N-(4,4'-dimethoxytrityl)-D(+)-biotinolyl)methoxymorpholinophosphine 
• 69705-14-2 5-((3a5,45,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl)pentyl 4-methylbenzenesulfonate 
• 1365259-06-8 (3aS,4S,6aR)-4-(5-hydroxypentyl)-1,3-bis(4-methoxybenzyl)tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one 
• 1365259-07-9 (3aS,4S,6aR)-1,3-bis(4-methoxybenzyl)-4-[5-(prop-2-en-1-yloxy)pentyl]tetrahydro-1H-thieno[3,4-d]imidazol-2(3H)-one 
• 1365259-09-1 methyl 6-({5-[(3aS,4S,6aR)-1,3-bis(4-methoxybenzyl)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentyl}oxy)hexanoate 
• 78757-38-7 cis-3,4-di(methoxycarbonylamino)-2-(δ-methoxycarbonylbutyl)thiophane 
• 58-85-5 (+/-)-biotin 

Relevant academic research and scientific papers

β-Keto and β-hydroxyphosphonate analogs of biotin-5′-AMP are inhibitors of holocarboxylase synthetase

Holocarboxylase synthetase (HLCS) catalyzes the covalent attachment of biotin to cytoplasmic and mitochondrial carboxylases, nuclear histones, and over a hundred human proteins. Nonhydrolyzable ketophosphonate (β-ketoP) and hydroxyphosphonate (β-hydroxyP) analogs of biotin-5′-AMP inhibit holocarboxylase synthetase (HLCS) with IC50 values of 39.7 μM and 203.7 μM. By comparison, an IC50 value of 7 μM was observed with the previously reported biotinol-5′-AMP. The Ki values, 3.4 μM and 17.3 μM, respectively, are consistent with the IC50 results, and close to the Ki obtained for biotinol-5′-AMP (7 μM). The β-ketoP and β-hydroxyP molecules are competitive inhibitors of HLCS while biotinol-5′-AMP inhibited HLCS by a mixed mechanism.

Expanding the substrate tolerance of biotin ligase through exploration of enzymes from diverse species

Technologies that enable the site-specific conjugation of chemical probes onto proteins are extremely useful for applications in cell biology and proteomics. We cloned, expressed, and purified biotin ligases from nine different species and screened them for the ability to ligate unnatural analogues of biotin onto the human p67 biotin acceptor domain. We discovered that the biotin ligases of Saccharomyces cerevisiae (yeast) and Pyrococcus horikoshii could accept alkyne and azide derivatives of biotin, respectively. HPLC, gel-shift, and mass spectrometry assays confirmed that these ligation reactions were ATP- and enzyme-dependent, as well as site-specific. We used the P. horikoshii-catalyzed azide ligation reaction to site-specifically introduce a phosphine probe onto p67 using the Staudinger ligation. These new ligation reactions demonstrate the differential substrate specificities of biotin ligases from different organisms and open the door to novel protein labeling applications. Copyright

Design, synthesis, and biological evaluation of biotinylated colchicine derivatives as potential antitumor agents

Chemical drug design based on the biochemical characteristics of cancer cells has become an important strategy for discovering new anti-tumour drugs to improve tumour targeting effects and reduce off-target toxicities. Colchicine is one of the most promin

BIOPROBES FOR LYSYL OXIDASES AND USES THEREOF

The present invention relates to novel bioprobes which are capable of binding to certain amine oxidase enzymes. These bioprobes are useful in methods of detecting and determining the concentration of certain amine oxidase enzymes in a sample as well as in methods for the quantitative assessment of inhibition of certain amine oxidases.

Azoacetylenes for the Synthesis of Arylazotriazole Photoswitches

We report a modular approach toward novel arylazotriazole photoswitches and their photophysical characterization. Addition of lithiated TIPS-acetylene to aryldiazonium tetrafluoroborate salts gives a wide range of azoacetylenes, constituting an underexplored class of stable intermediates.In situdesilylation transiently leads to terminal arylazoacetylenes that undergo copper-catalyzed cycloadditions (CuAAC) with a diverse collection of organoazides. These include complex molecules derived from natural products or drugs, such as colchicine, taxol, tamiflu, and arachidonic acid. The arylazotriazoles display near-quantitative photoisomerization and long thermalZ-half-lives. Using the method, we introduce for the first time the design and synthesis of a diacetylene platform. It permits implementation of consecutive and diversity-oriented approaches linking two different conjugants to independently addressable acetylenes within a common photoswitchable azotriazole. This is showcased in the synthesis of several photoswitchable conjugates, with potential applications as photoPROTACs and biotin conjugates.

Site-Selective Modification of Peptides and Proteins via Interception of Free-Radical-Mediated Dechalcogenation

The development of site-selective chemistry targeting the canonical amino acids enables the controlled installation of desired functionalities into native peptides and proteins. Such techniques facilitate the development of polypeptide conjugates to advance therapeutics, diagnostics, and fundamental science. We report a versatile and selective method to functionalize peptides and proteins through free-radical-mediated dechalcogenation. By exploiting phosphine-induced homolysis of the C?Se and C?S bonds of selenocysteine and cysteine, respectively, we demonstrate the site-selective installation of groups appended to a persistent radical trap. The reaction is rapid, operationally simple, and chemoselective. The resulting aminooxy linker is stable under a variety of conditions and selectively cleavable in the presence of a low-oxidation-state transition metal. We have explored the full scope of this reaction using complex peptide systems and a recombinantly expressed protein.

LIGAND LINKER SUBSTRATE

Ligand functionalized substrate including a solid substrate, which has been modified to provide grafted catching ligand groups covalently bound via a linker, methods of preparing said ligand functionalized substrate and the use thereof, such as to increase binding rate and the dynamic binding capacity (DBC).

SYNTHETIC RECEPTORS FOR IONOPHORIC COMPOUNDS

The present invention relates to synthetic receptors for ionophoric compounds, such as ionophoric toxins. Hence, the invention provides synthetic molecules capable of binding different ionophoric compounds, thereby being suitable for use in the detection,

Design and synthesis of biotinylated cardiac glycosides for probing Nur77 protein inducting pathway

The orphan nuclear receptor Nur77 (also known as TR3 or nerve growth factor-induced clone B NGFI-B) functions as a nuclear transcription factor in the regulation of target gene expression and plays a critical role in the regulation of differentiation, proliferation, apoptosis, and survival of many different cell types. Recent studies demonstrate that Nur77 also involves many important physiological and pathological processes including cancer, inflammation and immunity, cardiovascular diseases, and bone diseases. Our previous studies showed that cardiac glycosides could induce the expression of Nur77 protein and its translocation from the nucleus to the cytoplasm and subsequent targeting to mitochondria, leading to apoptosis of cancer cells. In order to probe the Nur77 protein inducting pathway, we designed and synthesized a series of novel biotinylated cardiac glycosides from β-Antiarin and α-Antiarin, two typical cardiac glycosides from the plant of Antiaris toxicaria. The induction of Nur77 protein expression of these biotinylated cardiac glycosides and their inhibitory effects on NIH-H460 cancer cell proliferation were evaluated. Results displayed that some biotinylated cardiac glycosides could significantly induce the expression of Nur77 protein comparable with their parent compounds β-Antiarin and α-Antiarin. Also, their streptavidin binding activities were evaluated. Among them, biotinylated cardiac glycosides P4b and P5a exhibited significant effect on the induction of Nur77 expression along with high binding capacity with streptavidin, suggesting that they can be used as probes for probing Nur77 protein inducting pathway.

Chemoselective triazole-phosphonamidate conjugates suitable for photorelease

Herein, we describe a new method for the conjugation of azide-containing target compounds that can be readily released as amines by irradiation with near UV light. This concept is based on a two-step protocol employing the chemoselective CuAAC and Staudinger-phosphonite reactions to deliver photo-cleavable phosphonamidate conjugates in high yields starting from 2-nitrobenzyl substituted phosphonites.