4753-07-5Relevant articles and documents
Synthesis and galectin-binding activities of mercaptododecyl glycosides containing a terminal β-galactosyl group
Murakami, Teiichi,Yoshioka, Kyoko,Sato, Yukari,Tanaka, Mutsuo,Niwa, Osamu,Yabuki, Soichi
, p. 1265 - 1269 (2011)
Mercaptododecyl glycosides containing a terminal β-galactosyl group were prepared from d-galactose or from d-lactose via hexa-O-acetyl-lactal (10) as a key intermediate. Interactions of these glycolipids (5 kinds) and galectins (β-galactoside binding lectins, 6 species) were evaluated by surface plasmon resonance (SPR) method. High binding responses were observed for the lactoside, 2-deoxy-lactoside, and lactosaminide with some galectins (Gal-3, -4, -8), whereas the galactoside and 2,3-dideoxy-lactoside showed low binding activities.
Glysosylation of nucleophiles on ion-exchange resin: A new synthesis of dibenzyl glycosyl phosphates
Nazarova,Shpirt,Orlova,Kononov
, p. 1202 - 1204 (2015)
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Halogenation and anomerization of glycopyranoside by TESH/bromine and BHQ/bromine
Xu, Lai,Luo, Chin-Hung,Chen, Chien-Sheng
, p. 315 - 321 (2020/07/13)
Treatment of peracetylated glycosides and β-isopropyl glycosides with halogen in the presence of TESH and BHQ has been found to result in the halogenation and the anomerization, respectively. Peracetylatedglycosides treaded with I2/TESH or Br2/TESH leading tothe formation of corresponding glycosyl halides, and b-isopropyl glycosidesreacted with Br2/BHQ resulting in the formation of a-glycosides. The anomerizationof glycosidic bond was considered to be catalyzed by in situ formation of hydrogenbromide from the mixing of Br2/BHQ.
A Sweet H2S/H2O2Dual Release System and Specific Protein S-Persulfidation Mediated by Thioglucose/Glucose Oxidase
Ni, Xiang,Li, Xiaolu,Shen, Tun-Li,Qian, Wei-Jun,Xian, Ming
, p. 13325 - 13332 (2021/09/03)
H2S and H2O2 are two redox regulating molecules that play important roles in many physiological and pathological processes. While each of them has distinct biosynthetic pathways and signaling mechanisms, the crosstalk between these two species is also known to cause critical biological responses such as protein S-persulfidation. So far, many chemical tools for the studies of H2S and H2O2 have been developed, such as the donors and sensors for H2S and H2O2. However, these tools are normally targeting single species (e.g., only H2S or only H2O2). As such, the crosstalk and synergetic effects between H2S and H2O2 have hardly been studied with those tools. In this work, we report a unique H2S/H2O2 dual donor system by employing 1-thio-β-d-glucose and glucose oxidase (GOx) as the substrates. This enzymatic system can simultaneously produce H2S and H2O2 in a slow and controllable fashion, without generating any bio-unfriendly byproducts. This system was demonstrated to cause efficient S-persulfidation on proteins. In addition, we expanded the system to thiolactose and thioglucose-disulfide; therefore, additional factors (β-galactosidase and cellular reductants) could be introduced to further control the release of H2S/H2O2. This dual release system should be useful for future research on H2S and H2O2.