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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Interaction of insulin with a triblock copolymer of PEG-(fumaric-sebacic acids)-PEG: Thermodynamic and spectroscopic studies
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Interaction of insulin with a triblock copolymer of PEG-(fumaric-sebacic acids)-PEG: Thermodynamic and spectroscopic studies

机译：胰岛素与PEG-（富马酸-癸二酸）-PEG的三嵌段共聚物的相互作用：热力学和光谱学研究

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A comparative study on the interaction of (PEG-co-P(FA/SQ-co-PEG) triblock copolymer with bovine and human insulins was carried out using isothermal titration calorimetry (ITC), circular dichroism (CD), and fluorescence spectroscopy. ITC data show that the copolymer has a low affinity for both proteins, with an association constant of about 7-9 x 10(3) M-1. Results also show that binding is enthalpically -driven, and disfavored by conformational entropy. CD spectroscopy studies reveal a small increase in the helical content and a decrease in -structure as well as random coil in both proteins. Acrylamide quenching experiments display reduced accessibility of tyrosines, while intrinsic fluorescence spectra show lower tyrosine emission. Furthermore, thermal unfolding experiments, studied by far-UV CD at 222 and 217 nm, demonstrate that upon interaction with the copolymer helix structure becomes less stable while the stability of -structure remains unchanged. Altogether, these observations indicate that (PEG-co-P(FA/SC)-co-PEG) triblock copolymer has similar effect(s) on both proteins. (C) 2007 Elsevier B.V All rights reserved.
机译：（PEG-co-P（FA / SQ-co-PEG）三嵌段共聚物与牛胰岛素和人胰岛素的相互作用的比较研究是使用等温滴定量热（ITC），圆二色性（CD）和荧光光谱法进行的。 ITC数据表明，该共聚物对两种蛋白均具有低亲和力，缔合常数约为7-9 x 10（3）M-1，结果还表明，结合是焓驱动的，并且受到构象熵的不利影响。研究表明，两种蛋白质的螺旋含量都有少量增加，结构减少，并且无规卷曲;丙烯酰胺淬灭实验显示酪氨酸的可及性降低，而固有荧光光谱显示酪氨酸的发射降低。 222和217 nm处的远紫外CD证明，在与共聚物相互作用后，螺旋结构变得较不稳定，而-结构的稳定性保持不变。表明（PEG-co-P（FA / SC）-co-PEG）三嵌段共聚物对两种蛋白质具有相似的作用。 （C）2007 Elsevier B.V保留所有权利。

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