Sialic acid (SA) is a widely distributed monosaccharide in animal tissues, plants, fungi, yeasts and bacteria. SA is commonly found as a terminal structure on complex carbohydrates having important functions such as cell-adhesions through various membrane bound lectins or bacterial and viral receptor proteins. Synthetic SA analogs with increased affinities could for example be used to block such interations1. They can be used as inhibitors of sialidase and sialyltransferase activities which makes them potential targets for drug developments2,3.
Studies have demonstrated that modification in position O-9 and O-5 could increase affinities for several siglecs4 and C-type lectins5. To identify new and more diverse set of high affinity analogs we adopted a rather un-bias approach by designing a scaffold based on a triazole structure with variable groups intended to mimic the functional groups of SA.
Computational docking studies, combinatorial OBOC synthesis6 (see figure), library screening with solublized and labeled glycan binding proteins and and statepof-the-art mass-spectrometry methosd are methodologies used in this project 6.
 L. Eyer, K. Hruska, Veterinarni Medicina, 2013, 58, 113–185
 K.H. Jung, R. Schworer, R.R. Schmidt, Trends Glycosci Glyc, 2003, 15, 275-289
 C. Büll, C.J. Boltje, M. Wassink, A.M.A. de Graaf, F.L. van Delft, M.H. den Brok, G.J. Adema, Mol Cancer Res, 2013, 12, 1935-1946
 O. Blixt, S.F. Han, L. Liao, Y. Zeng, J. Hoffmann, S. Futakawa, J.C. Paulson, J. Am. Chem. Soc., 2008, 130, 6680-6681
 G.A. Rabinovich, D.O. Croci, Immunity, 2012, 36, 322-335
 S.K. Kracun, E. Clo, H Clausen, S.B. Levery, K.J. Jensen, O. Blixt, J Proteome Res, 2010, 9, 6705-6714.