Bittencourt D, Souto B M, Verza N C, Vinecky F, Dittmar K, Silva P I, Andrade A C, da Silva F R, Lewis R V, Rech E L
Instituto de Ciências Biológicas, Departamento de Biologia Celular, Universidade de Brasília, Brasília-DF, Brazil.
Comp Biochem Physiol B Biochem Mol Biol. 2007 Aug;147(4):597-606. doi: 10.1016/j.cbpb.2007.03.013. Epub 2007 Apr 6.
Spiders produce up to six different kinds of silk, each one for a specific biological function. Spider silks are also known for their unique mechanical properties. The possibility of producing new materials with similar properties motivated research on these silk proteins (spidroins). Using expression sequence tags, we identified four spidroins produced by major ampullate, minor ampullate, flagelliform and tubuliform silk glands from the Brazilian spider Nephilengys cruentata (Araneae: Nephilidae). The new protein sequences showed substantial similarity to other spidroins previously described, with high content of alanine and glycine due to the presence of the highly repetitive motifs (polyAla, (GA)n, (GGX)n, (GPGGX)n). Similarities among sequences were also observed between the different spidroins with the exception of tubuliform spidroin, which presents a unique complex amino acid sequence with high amounts of serine and low amounts of glycine.
蜘蛛能产生多达六种不同类型的丝，每种丝都有特定的生物学功能。蜘蛛丝还因其独特的机械性能而闻名。生产具有类似性能的新材料的可能性推动了对这些丝蛋白（蜘蛛丝蛋白）的研究。利用表达序列标签，我们从巴西蜘蛛Nephilengys cruentata（蜘蛛目：园蛛科）的主要壶腹状腺、次要壶腹状腺、鞭毛状腺和管状腺中鉴定出了四种蜘蛛丝蛋白。新的蛋白质序列与先前描述的其他蜘蛛丝蛋白有很大的相似性，由于存在高度重复的基序（聚丙氨酸、(GA)n、(GGX)n、(GPGGX)n），丙氨酸和甘氨酸含量很高。除了管状蜘蛛丝蛋白外，不同蜘蛛丝蛋白之间的序列也存在相似性，管状蜘蛛丝蛋白呈现出独特的复杂氨基酸序列，丝氨酸含量高而甘氨酸含量低。
