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Galectins are a family of endogenous lectins with adhesion growth-regulatory activity binding galactosides. They are also known to play important roles in cancer, inflammation and a lot of other biological processes. Because of such features characterisation of galectin-carbohydrate interactions and identification of binding sites is of crucial importance for drug design. In the present study rat galectin-5 (rGal5) peptides containing key amino acids involved in carbohydrate binding were identified by CREDEX-MS of rGal5 and lactose - in complete agreement with the binding sites of the molecular modelling structure. Until now there are no X-Ray and NMR structures available for galectin-5 therefore studying galectin-5-carbohydrate interaction is very interesting. Both identified carbohydrate-binding peptides were synthesized and their affinity for lactose was demonstrated by affinity-MS.To get a more detailed view on the affinity and interaction kinetics of the CRD peptides and full galectin-5 with lactose SAW-bioaffinity measurements were performed. For real-time study of carbohydrate-lectin interaction a newly developed online-coupling of surface-acoustic wave measurements with ESI-Ion Trap MS was used. With this system the peptides interacting with on chip bound carbohydrate can be directly measured, enabling real time studies of peptide/protein-carbohydrate interactions.

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Frederike Eggers was born 1985 in Lörrach, on the border to Switzerland. Since 2005 she studied chemistry in Konstanz, Germany. There she took a great interest in analytical biochemistry what could be also seen in the present MSc Thesis. In 2011 she started her PhD in the Laboratory of Analytical Chemistry and Biopolymer Structure Analysis.

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