Glycosylation is crucial to a variety of biological processes including bacterial pathogenesis, cell signaling, tumor cell metastasis and neuronal development. These processes are characterized by the presence or the dynamic emergency of a clycosignature, that is, a specific and highly conserved pattern glycosylation. Thus, the development of reagents capable of targeting a specific glycan with high affinity and specificity has applications both in diagnostic and in therapy of diseases, and as specific reagents for glycomics.Here, we describe a novel approach to the design of a family of high affinity artifical carbohydrate-binding proteins (lectins) with tunable selectivity. We used rational design in conjunction with directed evloution techniques to evolve several artifical liceins with different specificity, thus capable of binding to different oligosaccharides of biological importanc. In our first application, we have selected varians that bind to TF, a cancer antigen, with high affinity. Further applications will include the use of selected artifical lectins as antiviral agents.
|Original language||English (US)|
|State||Published - Aug 31 2006|