Synthesis and conformational preferences of short analogues of antifreeze glycopeptides (AFGP)

• Małgorzata Urbańczyk,
• Michał Jewgiński,
• Joanna Krzciuk-Gula,
• Jerzy Góra,
• Rafał Latajka and
• Norbert Sewald

Beilstein J. Org. Chem. 2019, 15, 1581–1591, doi:10.3762/bjoc.15.162

• ., in food industry and biomedicine. Keywords: antifreeze glycopeptides; conformational preferences; NMR; PP II; solid phase synthesis; Introduction Certain species of polar and sub-polar fish created evolutionary strategies to survive in water at temperatures below the colligative freezing point

• the saccharide moiety is conformationally well-defined by the peptide backbone and the whole structure adopts a polyproline II (PP II) helix [17]. Antifreeze activity strongly relies on the stereochemistry of the amino acid residues. Earlier studies have shown that AFGP analogues containing either an

• 2-acetamido-2-deoxy-ᴅ-galactopyranosyl residue (ᴅ-GalNAc) attached to an allo-threonine-containing PP II helical peptide or containing ᴅ-GalNAc attached to a fully ᴅ-configured PP II helical peptide (retro-inverso) are inactive, while the corresponding ʟ-configured peptide showed antifreeze activity