335162-25-9Relevant articles and documents
Glycosylated Platinum(IV) Complexes as Substrates for Glucose Transporters (GLUTs) and Organic Cation Transporters (OCTs) Exhibited Cancer Targeting and Human Serum Albumin Binding Properties for Drug Delivery
Ma, Jing,Wang, Qingpeng,Huang, Zhonglv,Yang, Xiande,Nie, Quandeng,Hao, Wenpei,Wang, Peng George,Wang, Xin
supporting information, p. 5736 - 5748 (2017/07/22)
Glycosylated platinum(IV) complexes were synthesized as substrates for GLUTs and OCTs for the first time, and the cytotoxicity and detailed mechanism were determined in vitro and in vivo. Galactoside Pt(IV), glucoside Pt(IV), and mannoside Pt(IV) were highly cytotoxic and showed specific cancer-targeting properties in vitro and in vivo. Glycosylated platinum(IV) complexes 5, 6, 7, and 8 (IC50 0.24-3.97 μM) had better antitumor activity of nearly 166-fold higher than the positive controls cisplatin (1a), oxaliplatin (3a), and satraplatin (5a). The presence of a hexadecanoic chain allowed binding with human serum albumin (HSA) for drug delivery, which not only enhanced the stability of the inert platinum(IV) prodrugs but also decreased their reduction by reductants present in human whole blood. Their preferential accumulation in cancer cells compared to noncancerous cells (293T and 3T3 cells) suggested that they were potentially safe for clinical therapeutic use.
Montmorillonite K-10 as a reusable catalyst for fischer type of glycosylation under microwave irradiation
Bordoloi, Manobjyoti
, p. 300 - 308 (2008/12/21)
Montmorillonite K-10-catalyzed Fischer type glycosylation was studied for various monosacharides with different alcohols under microwave irradiation. The method was found to be efficient, economic, simple, and time saving and the catalyst montmorillonite K-10 was reused three times without loss of catalytic activity and anomeric selectivity. With glycerol, the method gave products glycosylated at primary alcohols only.
Chemo-enzymatic synthesis of polyhydroxyazepanes
Andreana, Peter R.,Sanders, Tom,Janczuk, Adam,Warrick, Joshua I.,Wang, Peng George
, p. 6525 - 6528 (2007/10/03)
Galactose oxidase (EC 1.1.3.9, GAO) is an extracellular copper-containing enzyme that utilizes molecular oxygen to convert the C6-primary hydroxyl moiety of D-galactopyranosides to hydrated aldehydes. Subsequent dehydratative coupling with hydroxylamines produces oximes (3a-f), which, when subjected to conditions of hydrogenolysis, give rise to polyhydroxyazepanes (11-17).