本文選題：ACE + C-domain選擇性抑制肽　； 參考：《食品科學(xué)》2017年05期

【摘要】：IW(Ile-Trp)、VW(Val-Trp)是兩種對(duì)人體體細(xì)胞ACE(somatic ACE,s ACE)中的C-結(jié)構(gòu)域(C-domain)具有選擇抑制性活性的食源性二肽,但其與ACE兩個(gè)結(jié)構(gòu)域(包括C-domain和N-domain)的結(jié)合模式與分子機(jī)制尚不明確。本實(shí)驗(yàn)采用分子柔性對(duì)接技術(shù)分別對(duì)上述兩種肽與靶標(biāo)的作用位點(diǎn)、結(jié)合能及作用力類(lèi)型等進(jìn)行研究。對(duì)接結(jié)果表明,IW、VW與ACE C-domain的活性位點(diǎn)存在氫鍵、親水、疏水相互作用力及配位鍵,與N-domain作用模式相似,但生成氫鍵數(shù)目較少,且與Zn~(2+)不產(chǎn)生靜電相互作用。通過(guò)比較IW、VW分別與兩個(gè)結(jié)構(gòu)域結(jié)合的能量差異,證明IW、VW針對(duì)兩個(gè)結(jié)構(gòu)域有不同的抑制強(qiáng)度,可為指導(dǎo)開(kāi)發(fā)ACE C-domain選擇性抑制肽提供理論參考。
[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.
【作者單位】： 上海理工大學(xué)醫(yī)療器械與食品學(xué)院;上海海事大學(xué)信息工程學(xué)院;江蘇長(zhǎng)壽集團(tuán)有限公司;內(nèi)蒙古燕谷坊生態(tài)農(nóng)業(yè)發(fā)展(集團(tuán))有限公司;國(guó)家糧食局科學(xué)研究院;
【基金】：上海市自然科學(xué)基金項(xiàng)目(14ZR1419200)
【分類(lèi)號(hào)】：R972
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本文編號(hào)：1800537