Saccharide/protein interaction

Meyer, J. E. W. and Schulz, G. E. (1997). Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from statistical analysis of saccharide-protein interactions, Protein Set, 6, 1084—1091. 

R. Fletterick The structure of maltoheptaose on phosphorylase by X-ray diffraction and the nature of saccharide-protein interaction B. A. Dmitriev Microbial O-antigenic hexosaminoglycans... 

Keywords CD mobility, Gene delivery, Multivalent interaction, Saccharide/protein interaction, Supramolecular dissociation... 

A review on saccharide-protein interactions by Prestegard et aF discusses the use of NMR to structurally characterise biologically important systems. It... 

To mimic saccharide-protein interactions, some PEG-polyrotaxanes were synthesized in Yui s group [38-40]. In these polyrotaxane, many binding ligands were introduced to the CD rings. High association constants were found between these polyrotaxanes and proteins such as concanavalin A and streptavidin. 

The same group modified the linker by using different numbers of carbon atoms (1, 5, 10) to afford variations of the local saccharide concentrations at the dendrimer surface.418 This study was aimed to determine the influence of this linker parameter on the glycodendrimer-protein interactions, the relationship between structure and water solubility, and to investigate amphiphilic properties. 

As polyanionic saccharides, heparinoids interact with a high number of proteins, the so-called heparin binding proteins. Heparinoid - protein interactions have usually been described for in vitro systems, and their physiological relevance is not always clear. On the other hand, heparinoids can influence biological systems, but in most cases the molecular basis is not fully understood. For this reason, interactions with proteins and biological properties of heparinoids will be discussed separately in the following. As heparinoid - protein interactions have been reviewed [3] the focus will be in rather short form on those areas in which heparinoid mimetics have been investigated. 

Many of the lipids found in nature are intimately bound to proteins and saccharides. The interactions within such structures are usually weak, but covalent bonds can occur (e.g., lipid inclusion in amylose or some lipid fractions in fish muscle tissue). During the processing and storage of food, the lipids are released and new bonds... 

Figure 8 Multivalency in carbohydrate-protein interactions can occur once a lectin with clustered sugar-binding sites and a multivalent saccharide are involved. Depending on the structural and conformational properties of a saccharide, the carbohydrate-protein interaction can be monovalent or multivalent (here divalent). Moreover, binding can occur either intra- or intermolec-ularly.

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