植物發展出各種不同的防衛策略來抵禦各種不同的病蟲害，有趣的是許多小分子量、鹼性及富含半胱胺酸(cysteine-rich)的蛋白質都和這些防禦機制有關，這些植物防禦蛋白包括hevein, thionins, knottin-like peptides,植物非專一性脂質運輸蛋白質(plant non-specific lipid transfer proteins, nsLTPs)和植物防禦素(plant defensins)，他們的結構含有2-6個雙硫鍵，形成一個緊密的折疊方式，其中，非專一性脂質運輸蛋白質和植物防禦素都有八個高度保留(conserved)的半胱胺酸，形成四個雙硫鍵。
非專一性脂質運輸蛋白質最為人所熟知的是能和各種脂質分子結合與試管內(in vitro)實驗中細胞膜之間運送脂質分子的能力，他們還被認為和其他的生物功能有關，包括病原菌的防禦、植物角質的生成和植物抵抗乾旱溫度變化之類的環境壓力的機制。非專一性脂質運輸蛋白質依據分子量，可以分成兩個不同類型，第一型(nsLTP1)的分子量約九千道耳吞(9kDa)，第二型(nsLTP2)的分子量約七千道耳吞(7kDa)，我們從稻米的種子中純化出第一和第二型的非專一性脂質運輸蛋白質，並進行鑑別、脂質運輸和脂質結合的特性分析。
植物防禦素最有名的則是他們有廣泛抵抗植物病原菌的能力，他們是一個鹼性、富含半胱胺酸、45到54個胺基酸大小的多肽族群，可以在各種不同植物中，包括小麥、大麥、豌豆、蘿蔔、高粱和綠豆中純化出來，除了可以抗菌外，植物防禦素也有其他的生物功能，包括抑制alpha-澱粉酶(alpha-amylase)、抑制胰蛋白酶(trypsin)、抑制鈉離子通道(sodium channel)和無細胞系統(cell-free system)中抑制蛋白質合成(protein synthesis)的各種不同活性。最近有個綠豆防禦素VrD1被報導在試管內(in vitro)實驗中具有抵抗豆象(bruchid)的抗蟲能力，我們利用核磁共振(Nuclear Magnetic Resonance, NMR)解出VrD1的三級結構，並確認它有抑制麵包蟲(Tenebrio molitor) alpha-澱粉酶的活性，這顯示VrD1可能是藉由抑制澱粉酶的機制達到抗蟲的功能，我們並比較序列和結構上的不同，並透過電腦模擬來討論VrD1和alpha-澱粉酶的可能的結合模式，這樣的結果將有助於改進VrD1的抗蟲效果。

Plants have developed various defense strategies against insect, bacterial and fungal attack. Interestingly, many small, highly basic and cysteine-rich proteins are involved in the defense mechanisms. These defense related proteins include hevein, thionins, knottin-like peptides, plant non-specific lipid transfer proteins (nsLTPs) and plant defensins. All of them adopt a compact fold stabilized by 2-6 disulfide bonds. Among these defense proteins, both nsLTPs and plant defensins have eight conserved cysteines forming four disulfide bonds.
NsLTPs are well known for their ability to bind a variety of lipid molecules and catalyze the transfer of lipids between membranes in vitro. They are also involved in other biological functions such as involvement in defense against pathogens, biosynthesis of cutin, and managing abiotic stress conditions imparted by temperature and drought situation. NsLTPs are subdivided into two different isoforms with molecular mass of 9kDa (nsLTP1) and 7kDa (nsLTP2). We have isolated nsLTP1 and nsLTP2 from rice seeds. Here, the purification, characterization, lipid-transfer and lipid-binding of nsLTPs are reported.
Plant defensins are well known for their ability to exhibit antifungal activity against a broad range of fungi including various plant pathogens. They are a family of cysteine-rich, basic peptides of 45 to 54 amino acids isolated from many plants including wheat, barley, pea, radish, sorghum and mung bean. Plant defensins also have additional biological activities including inhibition of alpha-amylase, of trypsin, of sodium channel and of protein synthesis in cell-free system. Recently, an insecticidal plant defensin designated VrD1 was reported exhibiting in vitro insect-resistant activity against bruchid. Here we report the three-dimensional structure of VrD1 as determined by NMR spectroscopy. Furthermore, VrD1 was confirmed to inhibit Tenebrio molitor alpha-amylase implying that VrD1 exhibited insecticidal activity through inhibition of alpha-amylase. Computational docking experiments were used to study the interactions between VrD1 and insect alpha-amylase, and these results provide useful interaction information that may improve the insecticidal activity of VrD1.

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