Beilstein J. Org. Chem.2019,15, 1581–1591, doi:10.3762/bjoc.15.162
, Department of Chemistry, Bielefeld University, Universitätsstraße 25, Bielefeld, D-33615, Germany 10.3762/bjoc.15.162 Abstract Antifreeze glycoproteins are a class of biological agents which enable living at temperatures below the freezing point of the body fluids. Antifreezeglycopeptides usually consist
of repeating tripeptide unit (-Ala-Ala-Thr*-), glycosylated at the threonine side chain. However, on the microscopic level, the mechanism of action of these compounds remains unclear. As previous research has shown, antifreeze activity of antifreezeglycopeptides strongly relies on the overall
have shown a strong influence of the stereochemistry of amino acid residues on the peptide chain stability, which could be connected to the antifreeze activity of these compounds. A better understanding of the mechanism of action of antifreezeglycopeptides would allow applying these materials, e.g
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Graphical Abstract
Figure 1:
Glycosylated building blocks prepared for solid phase peptide synthesis (SPPS).
Beilstein J. Org. Chem.2012,8, 1657–1667, doi:10.3762/bjoc.8.190
Bielefeld, Germany 10.3762/bjoc.8.190 Abstract Antifreezeglycopeptides (AFGPs) are a special class of biological antifreeze agents, which possess the property to inhibit ice growth in the body fluids of arctic and antarctic fish and, thus, enable life under these harsh conditions. AFGPs are composed of 4
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Graphical Abstract
Scheme 1:
Synthesis of the monosaccharide-substituted threonine building block (A = allo-L-threonine; B = D-t...