**8. Conclusions and outlook**

While Nature has provided various organisms with peptides and glycopeptides to mitigate cellular damage during exposure to cold temperatures, these compounds have failed to be effective cryoprotectants in various medical and commercial applications. This is somewhat ironic as these compounds are potent inhibitors of ice recrystallization, a process that contrib‐ utes significantly to cellular injury. The recent discovery that IRI activity can be selectively enhanced while suppressing TH activity in various analogues of biological antifreezes is a significant advancement towards the rational design of novel cryoprotectants. Some of these molecules have even demonstrated the ability to enhance cell viabilities post-thaw. While these compounds do not yet exhibit viabilities comparable to 10 % DMSO solutions, it is feasible that with a better understanding of the structural features necessary for potent IRI activity future analogues will be efficient cryoprotectants replacing conventional ones such as DMSO and glycerol. The recent discovery that small molecules are extremely potent inhibitors of ice recrystallization represents a "quantum leap" forward in this area. Further studies with these compounds *in vitro* and *in vivo* will elucidate their effectiveness as cryoprotectants while overcoming the problems of high cost and large-scale synthesis associated with the higher molecular weight analogues of biological antifreeze that exhibit the potent IRI activity, a property necessary for an effective cryoprotectant.
