Abstract
A recently identified Antarctic fish protein termed antifreeze potentiating protein (AFPP) is thought to act as an adjunct to the previously characterised antifreeze glycoproteins (AFGPs), the two acting together to inhibit ice crystal growth in vivo. Elucidating the functional properties of the new AFPP requires access to large amounts of pure product, but the paucity of natural material necessitates alternative approaches. We therefore embarked on the total chemical synthesis of the AFPP, through a convergent ligation strategy. After many challenges, mostly due to the solubility issues of the peptide fragments, and several revisions of the original synthetic strategy, we have successfully synthesized a masked analogue of AFPP. The key to the successful synthesis was the use of a solubilising tag attached through a hydrolysable linker.
Highlights
Antarctic fishes survive in freezing seawater through the production of protective antifreeze proteins.[1]
Almost all Antarctic fish exposed to freezing seawater that we have analyzed to date, have internalized ice crystals sequestered in macrophages within the spleen.[4,5]
Since such crystals will contain adsorbed antifreeze potentiating protein (AFPP) and antifreeze glycoproteins (AFGPs), these observations raise the possibility that AFPP, in conjunction with AFGP, inhibits ice crystal growth in the blood but might promote removal of potentially lethal circulating ice crystals by facilitating uptake of the ice/antifreeze complexes into spleen macrophages
Summary
Antarctic fishes survive in freezing seawater (ca. −1.9 °C) through the production of protective antifreeze proteins.[1]. Mostly due to the solubility issues of the peptide fragments, and several revisions of the original synthetic strategy, we have successfully synthesized a masked analogue of AFPP.
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