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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Polyethyleneimine-protein interactions and implications on protein stability
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Polyethyleneimine-protein interactions and implications on protein stability

机译:聚乙烯亚胺-蛋白质相互作用及其对蛋白质稳定性的影响

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摘要

Protein stability assessment of seven model proteins in the presence of low molecular weight polyethyleneimine (PEI, MW 2000Da) was performed. Thermodynamic stability, monitored by circular dichroism (CD) spectroscopy, showed that the polymer did not have a major effect on the melting temperature (T_m) of the basic proteins - muscle lactate dehydrogenase (LDH), ribonuclease A, lysozyme and cutinase, while for the acidic ones - human growth hormone, human serum albumin and heart lactate dehydrogenase - there was a shift in T_m towards lower temperatures. The secondary structures of the basic proteins were essentially the same, with none or a slight increase in the CD spectra, in presence of the polymer. In the case of the acidic proteins, the CD spectra were diminished mostly due to phase separation. Assuming a homogeneous distribution of the net charge on the protein surface a quantitative inverse relationship was established between surface charge density of the acidic proteins and the PEI_(2000) concentration required for maximum flocculation. Despite lowering the thermal stability of acidic proteins, PEI_(2000) was seen to protect heart LDH at an increasing oxidative stress.
机译:在低分子量聚乙烯亚胺(PEI,分子量为2000Da)的存在下,对七个模型蛋白质的蛋白质稳定性进行了评估。通过圆二色性(CD)光谱监测的热力学稳定性表明,该聚合物对碱性蛋白质-肌肉乳酸脱氢酶(LDH),核糖核酸酶A,溶菌酶和角质酶的融解温度(T_m)没有重大影响。酸性物质-人类生长激素,人类血清白蛋白和心脏乳酸脱氢酶-T_m趋向于较低的温度。在存在该聚合物的情况下,碱性蛋白质的二级结构基本相同,CD光谱没有增加或仅有轻微增加。在酸性蛋白质的情况下,CD光谱主要由于相分离而减弱。假设净电荷在蛋白质表面的均匀分布,则酸性蛋白质的表面电荷密度与最大絮凝所需的PEI_(2000)浓度之间建立了定量的反比关系。尽管降低了酸性蛋白的热稳定性,PEI_(2000)仍被认为可以保护心脏LDH免受氧化应激的增加。

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