Organic & Biomolecular Chemistry Blog

The binding of two α-fucosylamide-based mimics of Lewis^X to DC-SIGN ECD (Dendritic Cell-Specific ICAM-3 Grabbing Nonintegrin extracellular domain) using STD NMR and docking studies has been investigated by Pedro M. Nieto and coworkers.  The mimics are shown to bind in a similar way to Lewis^X, through the fructose moiety and in a multi-modal fashion, but with increased affinity due to the aromatic moiety.

Insights into molecular recognition of Lewis^X mimics by DC-SIGN using NMR and molecular modelling
Cinzia Guzzi, Jesús Angulo, Fabio Doro, José J. Reina, Michel Thépaut, Franck Fieschi, Anna Bernardi, Javier Rojo and Pedro M. Nieto
Org. Biomol. Chem., 2011, 9, 7705-7712
DOI: 10.1039/C1OB05938F

While L-sugars are promising candidates in medicinal chemistry, such as L-ribose-containing nucleosides, only their D-forms naturally occur, thus prompting the need for an efficient synthetic methodology.

In this aim, Gaik-Khuan Chuah et al. at the National University of Singapore have devised a novel route to access rare L-lyxose and L-ribose in a simple 5-step procedure, leading to significantly increased yields and greener conditions as compared to previous reports.

To overcome the critical step for the oxidation of D-sugar to the corresponding D-lactone, the authors have used a heterogeneous catalyst – palladium-bismuth supported on carbon – and molecular oxygen, thus eliminating the need for bromine often used for this oxidation. The catalyst can easily be separated from the reaction mixture and reused, which enhances even further the relevance of this novel protocol.

Interested? Why not read this Hot Article now, it will be free to access for the next 4 weeks upon a simple registration process.

Reference
A heterogeneous Pd–Bi/C catalyst in the synthesis of L-lyxose and L-ribose from naturally occurring D-sugars
Ao Fan, Stephan Jaenicke and Gaik-Khuan Chuah
Org. Biomol. Chem., 2011, Advance Article
DOI: 10.1039/C1OB06116J, Paper

In this Hot article, Adam T. Slósarczyk and Lars Baltzer from Uppsala University, Sweden, report on the conjugation of designed polypeptides to a small organic molecule as a strategy for the recognition and binding of phosphorylated proteins.

Conjugating a polypeptide to the zinc chelating ligand led to a dramatic increase in affinity and selectivity towards phosphoproteins, here caseins, however this concept for binder development is thought to be widely applicable and ‘high-affinity binders can conveniently be developed for a variety of proteins including those with posttranslational modifications for which small molecule recognition elements are available.’, report the authors.

Curious to learn more? Read the full article now, FREE to access for the next 4 weeks.

Reference
The molecular recognition of phosphorylated proteins by designed polypeptides conjugated to a small molecule that binds phosphate
Adam T. Ślósarczyk and Lars Baltzer
Org. Biomol. Chem., 2011, Advance Article
DOI: 10.1039/C1OB06154B, Paper