Abstract
The role of hydration in modulating solution conformation, molecular recognition, and biological activity of oligosaccharides, proteins, and nucleotides is widely recognized but is often neglected when investigating many biological processes such as the mechanism by which biological antifreezes inhibit the growth of ice. We have investigated the relationship between carbohydrate configuration and recrystallization-inhibition (RI) activity in functional C-linked antifreeze glycoprotein (AFGP) analogues using a series of analogues 1−4. While analogues 1−4 did not show any thermal hysteresis (TH) activity, 1 did exhibit weak dynamic ice shaping indicating that this compound had the ability to interact with the ice lattice. The d-mannose and d-talose analogues (3 and 4, respectively) exhibited very weak RI activity with mean largest grain size values similar to phosphate buffered saline, the negative control. d-Glucose analogue 2 exhibited moderate RI activity while d-galactose analogue 1 was the most potent ...
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