ACEC-结构域选择性抑制二肽与ACE结构域的结合模式

发布时间：2018-04-25 08:24

  本文选题：ACE + C-domain选择性抑制肽　； 参考：《食品科学》2017年05期

【摘要】：IW(Ile-Trp)、VW(Val-Trp)是两种对人体体细胞ACE(somatic ACE,s ACE)中的C-结构域(C-domain)具有选择抑制性活性的食源性二肽,但其与ACE两个结构域(包括C-domain和N-domain)的结合模式与分子机制尚不明确。本实验采用分子柔性对接技术分别对上述两种肽与靶标的作用位点、结合能及作用力类型等进行研究。对接结果表明,IW、VW与ACE C-domain的活性位点存在氢键、亲水、疏水相互作用力及配位键,与N-domain作用模式相似,但生成氢键数目较少,且与Zn~(2+)不产生静电相互作用。通过比较IW、VW分别与两个结构域结合的能量差异,证明IW、VW针对两个结构域有不同的抑制强度,可为指导开发ACE C-domain选择性抑制肽提供理论参考。
[Abstract]:IWE-TRP is a food derived dipeptide with selective inhibitory activity to C-domain, a C-domain domain in human somatic cell ACE(somatic ACEs, but its binding pattern and molecular mechanism with two domains of ACE (including C-domain and N-domain) are unclear. Molecular flexible docking technique was used to study the interaction sites, binding energy and force types between the two peptides. The results show that there are hydrogen bonds, hydrophilic, hydrophobic and hydrophobic interaction forces and coordination bonds in the active sites of VW and ACE C-domain, which are similar to those of N-domain, but the number of hydrogen bonds is small, and no electrostatic interaction occurs with Zn~(2). By comparing the energy difference of IWV W binding with two domains, it is proved that IWN VW has different inhibition intensity for the two domains, which can provide a theoretical reference for the development of ACE C-domain selective inhibitory peptides.
【作者单位】： 上海理工大学医疗器械与食品学院;上海海事大学信息工程学院;江苏长寿集团有限公司;内蒙古燕谷坊生态农业发展(集团)有限公司;国家粮食局科学研究院;
【基金】：上海市自然科学基金项目(14ZR1419200)
【分类号】：R972
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本文编号：1800537