Insights into structure, affinity, specificity, and function of GAG-protein interactions through the chemoenzymatic preparation of defined sulfated oligohyaluronans
Author:
Schiller Jürgen1, Lemmnitzer Katharina1, Dürig Jan-Niklas2, Rademann Jörg2ORCID
Affiliation:
1. Faculty of Medicine , Institute of Medical Physics and Biophysics, University of Leipzig , Härtelstraße 16-18 , 04107 Leipzig , Germany 2. Department of Biology, Chemistry, and Pharmacy , Institute of Pharmacy, Pharmaceutical and Medicinal Chemistry, Freie Universität Berlin , Königin-Luise-Str. 2+4 , 14195 Berlin , Germany
Abstract
Abstract
High amounts of glycosaminoglycans (GAG) such as hyaluronan (HA) occur in connective tissues. There is nowadays increasing evidence that a “sulfation code” exists which mediates numerous GAG functions. High molecular weight and inhomogeneity of GAG, however, aggravated detailed studies. Thus, synthetic oligosaccharides were urgently required. We will review here chemoenzymatic and analytic strategies to provide defined sulfated and anomerically modified GAG oligosaccharides of the HA type. Representative studies of protein/GAG interactions by (bio)chemical and biophysical methods are reported yielding novel insights into GAG-protein binding. Finally, the biological conclusions and in vivo applications of defined sulfated GAG oligosaccharides will be discussed.
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
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