Latent Ice Recrystallization Inhibition Activity in Nonantifreeze Proteins: Ca2+-Activated Plant Lectins and Cation-Activated Antimicrobial Peptides.
Latent Ice Recrystallization Inhibition Activity in Nonantifreeze Proteins: Ca2+-Activated Plant Lectins and Cation-Activated Antimicrobial Peptides.
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DOI：
10.1021/acs.biomac.5b01118
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发表时间：
2015-10-12
影响因子：
6.2
通讯作者：
Gibson MI
中科院分区：
文献类型：
--
作者：
Mitchell DE;Gibson MI
生活在极地地区的生物进化出一系列抗冻蛋白(AFGP)，通过调节冰的结构使它们能够生存。这些蛋白质在细胞冷冻保存、抗冰表面、冷冻食品和冷冻外科等方面具有巨大的潜力，但它们的可用性相对较低，以及对其作用方式的质疑限制了它们的应用。这引发了对能够复制这种功能的仿生材料的研究。识别能够抑制冰生长的新结构和序列对于帮助我们理解这些蛋白质至关重要。在这里，我们证明了植物c型凝集素具有与人类c型凝集素相似的生物学功能(糖链识别)，但与AFP没有序列同源性，显示出钙依赖的冰再结晶抑制(IRI)活性。这种IRI活性可以通过改变钙离子浓度来开启/关闭。为了表明可能存在更多的(非抗冻剂)蛋白具有显示IRI的潜力，考虑了第二个基序，即两亲性。所有已知的AFP都定义了疏水/亲水结构域，使这一选择合理化。廉价和广泛使用的抗微生物Nisin被发现具有阳离子依赖的IRI活性，受酸或组氨酸结合离子(如锌或镍)的控制，这些离子促进了其两亲性结构。这些结果证明了一种新的鉴定抗冻蛋白模拟大分子的方法，并可能有助于人工合成AFP模拟分子的开发。
Organisms living in polar regions have evolved a series of antifreeze (glyco) proteins (AFGPs) to enable them to survive by modulating the structure of ice. These proteins have huge potential for use in cellular cryopreservation, ice-resistant surfaces, frozen food, and cryosurgery, but they are limited by their relatively low availability and questions regarding their mode of action. This has triggered the search for biomimetic materials capable of reproducing this function. The identification of new structures and sequences capable of inhibiting ice growth is crucial to aid our understanding of these proteins. Here, we show that plant c-type lectins, which have similar biological function to human c-type lectins (glycan recognition) but no sequence homology to AFPs, display calcium-dependent ice recrystallization inhibition (IRI) activity. This IRI activity can be switched on/off by changing the Ca2+ concentration. To show that more (nonantifreeze) proteins may exist with the potential to display IRI, a second motif was considered, amphipathicity. All known AFPs have defined hydrophobic/hydrophilic domains, rationalizing this choice. The cheap, and widely used, antimicrobial Nisin was found to have cation-dependent IRI activity, controlled by either acid or addition of histidine-binding ions such as zinc or nickel, which promote its amphipathic structure. These results demonstrate a new approach in the identification of antifreeze protein mimetic macromolecules and may help in the development of synthetic mimics of AFPs.