68681-00-5Relevant articles and documents
Exploring the Biochemical Foundations of a Successful GLUT1-Targeting Strategy to BNCT: Chemical Synthesis and in Vitro Evaluation of the Entire Positional Isomer Library of ortho-Carboranylmethyl-Bearing Glucoconjugates
Matovi?, Jelena,J?rvinen, Juulia,Sokka, Iris K.,Imlimthan, Surachet,Raitanen, Jan-Erik,Montaser, Ahmed,Maaheimo, Hannu,Huttunen, Kristiina M.,Per?niemi, Sirpa,Airaksinen, Anu J.,Sarparanta, Mirkka,Johansson, Mikael P.,Rautio, Jarkko,Ekholm, Filip S.
, p. 285 - 304 (2020/12/21)
Boron neutron capture therapy (BNCT) is a noninvasive binary therapeutic modality applicable to the treatment of cancers. While BNCT offers a tumor-targeting selectivity that is difficult to match by other means, the last obstacles preventing the full har
Exploring glycosylation reactions under continuous-flow conditions
Cancogni, Damiano,Lay, Luigi
, p. 2873 - 2878 (2015/01/16)
The industrial development of carbohydrate-based drugs is greatly thwarted by the typical challenges inherent in oligosaccharide synthesis. The practical advantages of continuous-flow synthesis in microreactors (high reproducibility, easy scalability, and fast reaction optimization) may offer an effective support to make carbohydrates more attractive targets for drug-discovery processes. Here we report a systematic exploration of the glycosylation reaction carried out under microfluidic conditions. Trichloroacetimidates and thioglycosides have been investigated as glycosyl donors, using both primary and secondary acceptors. Each microfluidic glycosylation has been compared with the corresponding batch reaction, in order to highlight advantages and drawbacks of microreactors technology. As a significant example of multistep continuous-flow synthesis, we also describe the preparation of a trisaccharide by means of two consecutive glycosylations performed in interconnected microreactors.
'Naked' and hydrated conformers of the conserved core pentasaccharide of N-linked glycoproteins and its building blocks
Barry, Conor S.,Cocinero, Emilio J.,Carcabal, Pierre,Gamblin, David P.,Stanca-Kaposta, E. Cristina,Remmert, Sarah M.,Fernandez-Alonso, Maria C.,Rudic, Svemir,Simons, John P.,Davis, Benjamin G.
, p. 16895 - 16903 (2013/12/04)
N-glycosylation of eukaryotic proteins is widespread and vital to survival. The pentasaccharide unit -Man3GlcNAc2- lies at the protein-junction core of all oligosaccharides attached to asparagine side chains during this process. Although its absolute conservation implies an indispensable role, associated perhaps with its structure, its unbiased conformation and the potential modulating role of solvation are unknown; both have now been explored through a combination of synthesis, laser spectroscopy, and computation. The proximal -GlcNAc-GlcNAc- unit acts as a rigid rod, while the central, and unusual, -Man-β-1,4-GlcNAc- linkage is more flexible and is modulated by the distal Man-α-1,3- and Man-α-1,6- branching units. Solvation stiffens the 'rod' but leaves the distal residues flexible, through a β-Man pivot, ensuring anchored projection from the protein shell while allowing flexible interaction of the distal portion of N-glycosylation with bulk water and biomolecular assemblies.
