Knight C A, Wen D, Laursen R A
National Center for Atmospheric Research, Boulder, Colorado 80307.
Cryobiology. 1995 Feb;32(1):23-34. doi: 10.1006/cryo.1995.1002.
Evidence is presented that the nonequilibrium antifreeze peptide (AFP) from winter flounder has a special ability to inhibit recrystallization in ice only when an appreciable amount of liquid is present, as is the case when the system contains salts and the temperature is not too low. In this circumstance the AFP binds to the ice surface at the ice-solution interfaces in grain boundaries, preventing migration of the solution and effectively immobilizing the boundaries. In the absence of liquid, recrystallization inhibition appears to be a common property of many peptides. This is consistent with the view that the special effects of AFPs require a structural fit onto ice, and therefore require the AFP molecules to have the mobility to achieve that fit. Since the concentration of salt required to induce the special recrystallization inhibition effects of AFPs is lower (< 10 mM) than that found normally in physiological fluids, AFPs could play a role in the survival of organisms by preventing damage due to recrystallization. The proposition that mobility is needed for AFP molecules to produce their special influence upon ice growth argues against any special effects of AFPs in devitrification.
有证据表明，冬季比目鱼的非平衡抗冻肽（AFP）具有一种特殊能力，即只有当存在相当数量的液体时，它才能抑制冰的再结晶，就像系统中含有盐且温度不太低时的情况一样。在这种情况下，AFP在晶界处的冰 - 溶液界面结合到冰表面，阻止溶液迁移并有效地固定边界。在没有液体的情况下，抑制再结晶似乎是许多肽的共同特性。这与以下观点一致，即AFP的特殊作用需要与冰有结构适配，因此要求AFP分子具有实现这种适配的流动性。由于诱导AFP产生特殊再结晶抑制作用所需的盐浓度（<10 mM）低于生理流体中通常发现的浓度，AFP可能通过防止再结晶造成的损害在生物体的存活中发挥作用。AFP分子需要流动性才能对冰生长产生特殊影响这一观点与AFP在玻璃化转变中的任何特殊作用相悖。
