羟喜树碱结合肽的结合作用分析

To search for homologous sequence mode of 10-Hydroxyl camptothecine binding peptides

目的:对羟喜树碱结合肽进行结合作用分析,为进一步研究阐明羟喜树碱的抗癌机制、耐药机制以及毒理机制提供帮助。方法:使用生物信息学软件对羟喜树碱结合肽序列进行比对分析,寻找羟喜树碱结合肽同源保守性模式,对羟喜树碱结合肽进行结合作用分析。结果:羟喜树碱结合肽原始序列的保守性模式为xxxxxLxPxxxx。其中L、P皆为疏水脂肪族氨基酸。依据氨基酸可以分为疏水脂肪族氨基酸、疏水芳香族氨基酸、极性带电氨基酸和极性不带电氨基酸的原则,分别以G、F、R、N四个符号来代表四大类氨基酸,对羟喜树碱结合肽原始序列进行了简并转换,羟喜树碱结合肽简并序列的保守性模式为xGxxGGGNxGGx。结论:预测羟喜树碱结合肽可能通过形成疏水口袋区与羟喜树碱发生相互作用,而疏水口袋中的易形成氢键的极性不带电氨基酸则可能与羟喜树碱形成氢键,进一步稳定加强其相互作用。

Object：To search for homologous sequence mode of lO-Hydroxyl camptothecine （HCPT） binding peptides and their binding mechanism, so as to offer help with researches on decoding the anticancer mechanism of HCPT,the mechanism underlying resistance to HCPT and the mechanism of its side effects. Method：The homologous sequence mode and binding effects of HCPT binding peptides were analyzed by bioinformatical software. Result ：The homologous sequence mode of original HCPT binding peptides was identified as xxxxxLxPxxxx while the homologous sequence mode of degeneracy HCPT binding peptides was identified as xGxxGGGNxGGx by sequence alignment analysis. The homologous sequence mode of HCPT binding peptides consisted of hydrophobic amino acid residues. Conclusion ： The HCPT binding peptides might form hydrophobic pockets to interact with HCPT and uncharged polar amino acid residues within the hydrophobic pockets would enhance the binding effects between HCPT and HCPT binding peptides by forming hydrogen bonds with HCPT.