Sugar-Modified Foldamers as Conformationally Defined and Biologically Distinct Glycopeptide Mimics

Aloysius Siriwardena (1) , Kiran Kumar Pulukuri (2) , Pancham S. Kandiyal (2) , Saumya Roy (1) , Omprakash Bande (1) , Subhash Ghosh (3) , José Manuel Garcia fernández (4) , Fernando Ariel martin (5) , Jean-Marc Ghigo (5) , Christophe Beloin (5) , Keigo Ito (6) , Robert J. Woods (7, 6) , Ravi Sankar Ampapathi (2) , Tushar Kanti Chakraborty (2)

1 LG - Laboratoire des Glucides
2 CSIR-CDRI - CSIR-Central Drug Research Institute
3 IICT - CSIR Indian Institute of Chemical Technology
4 Universidad de Sevilla / University of Sevilla
5 Génétique des Biofilms
6 University of Georgia [USA]
7 NUI Galway - National University of Ireland [Galway]

To fold or not to fold? It is shown that attached sugars play a defining role in the conformations adopted by a pair of novel SAA-derived foldamers in water and that these differences are reflected in the contrasting interactions of these glycofoldamers with various biological targets. C green, O red, N blue, H gray; yellow oval=mannose.

Keywords: neoglycopeptides; protein–carbohydrate interactions; restrained molecular dynamics; solution conformational preferences; glycofoldamers

Domains: Bacteriology

Aloysius Siriwardena, Kiran Kumar Pulukuri, Pancham S. Kandiyal, Saumya Roy, Omprakash Bande, et al.. Sugar-Modified Foldamers as Conformationally Defined and Biologically Distinct Glycopeptide Mimics. Angewandte Chemie International Edition, 2013, 52 (39), pp.10221 - 10226. ⟨10.1002/anie.201304239⟩. ⟨pasteur-01385432⟩