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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Monitoring thermal and chemical unfolding of Brugia malayi calreticulin using fluorescence and Circular Dichroism spectroscopy
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Monitoring thermal and chemical unfolding of Brugia malayi calreticulin using fluorescence and Circular Dichroism spectroscopy

机译：使用荧光和圆形二色性光谱监测Brugia Malayi Caltreticulin的热和化学展开

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摘要

Calreticulin of Brugia malayi (BmCRT) play very important role in host-parasite interaction. In previous study it was found that BmCRT is responsible for prevention of host classical complement pathway activation via its interaction with first component C1q of the human host. Therefore, BmCRT is an essential protein for parasite survival and an important drug target to fend filariasis. In the present study, we have carried out a systamatic biophysical characterization of BmCRT protein. Unfolding of BmCRT was found to be non-cooperative two-state process in the presence of both denaturant GdmCl and urea. The results also illustrated that protein lost its 50% activity at 1.5 M GdmCl and 3 M Urea. Partially unfolded and molten-globule like intermediate state was observed at 0.8 to 1.2 M GdmCl while Urea unfolding showed intermediate state at 1.2 to 1.6 M. Unfolding pathway monitored with the help of apolar quencher, favor above observations. All of these findings support the presence of detectable intermediate state during unfolding pathway of BmCRT. Furthermore, this study indicates that BmCRT is more stable toward temperature (Tm = 65 degrees C), pH and trypsin digestion. These differences in properties as compared to host can be fruitfully utilized for synthesis of compounds effective against the parasite. (C) 2017 Elsevier B.V. All rights reserved.
机译：Brugia Malayi（BMCRT）的Caltretitulin在宿主寄生虫相互作用中起着非常重要的作用。在先前的研究中，发现BMCRT通过其与人宿主的第一组分C1Q的相互作用，负责预防宿主经典补体途径激活。因此，BMCR是寄生物存活的必要蛋白质和一个围绕丝虫病的重要药物靶标。在本研究中，我们进行了BMCRT蛋白的系统性生物物理表征。在Denaturant GdMCL和尿素存在下，发现BMCRT的展开是非合作的两种过程。结果还说明蛋白质在1.5M GDMCL和3米尿素下失去了50％活性。在0.8-1.2M GdMCL下观察到部分展开和熔融 - 小球，如中间状态观察到，尿素展开在1.2-1.6M的中间状态下显示出在脱离猝灭剂的帮助下监测的展开途径，有利于上述观察结果。所有这些发现都支持BMCRT的展开途径期间存在可检测的中间状态。此外，该研究表明BMCRT对温度（TM = 65℃），pH和胰蛋白酶消化更稳定。与宿主相比，这些性质的差异可以效果效果地用于合成对寄生虫有效的化合物。 （c）2017年Elsevier B.V.保留所有权利。

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