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胰岛素在氧化锌量子点表面的展开。

Unfolding of insulin at the surface of ZnO quantum dots.

作者信息

Hosseinzadeh Ghader, Maghari Ali, Saboury Ali A, Moosavi-Movahedi Ali A

机构信息

Department of Physical Chemistry, School of Chemistry, College of Science, University of Tehran, Tehran, Iran.

Department of Physical Chemistry, School of Chemistry, College of Science, University of Tehran, Tehran, Iran.

出版信息

Int J Biol Macromol. 2016 May;86:169-76. doi: 10.1016/j.ijbiomac.2016.01.075. Epub 2016 Jan 23.

Abstract

ZnO quantum dots (QDs) have been used in many biomedical applications such as bioimaging, cancer treatments and etc. Crystallinity, particle size, optical absorption and photoluminescence spectra of ZnO QDs were analyzed by X-ray diffraction (XRD), transmission electron microscopy (TEM), UV-vis absorption spectroscopy and fluorescence spectroscopy respectively. Interaction of ZnO QDs with insulin was investigated by fluorescence quenching, circular dichroism (CD), isothermal titration calorimetry (ITC) and thermal aggregation tests. The fluorescence quenching results showed a static type quenching along with red shift in synchronize fluorescence (a sign of protein unfolding). CD spectroscopy results also confirmed this unfolding and show a reduction in alpha helices content of insulin in contact with ZnO QDs and their conversion to random coils. According to ITC results, the ΔG, ΔH and binding constant of this interaction are -32.35 kJ/mol, -43.21 kJ/mol and 4.69 × 10(5) M(-1), respectively. Thermal aggregation test showed fast aggregation of insulin in the presence of ZnO QDs. Therefore in biological application of ZnO QDs such as bioimaging, presence of such QDs in vicinity of insulin could unfold this protein.

摘要

氧化锌量子点(QDs)已被用于许多生物医学应用,如生物成像、癌症治疗等。分别通过X射线衍射(XRD)、透射电子显微镜(TEM)、紫外可见吸收光谱和荧光光谱对氧化锌量子点的结晶度、粒径、光吸收和光致发光光谱进行了分析。通过荧光猝灭、圆二色性(CD)、等温滴定量热法(ITC)和热聚集试验研究了氧化锌量子点与胰岛素的相互作用。荧光猝灭结果显示为静态猝灭,同时同步荧光出现红移(蛋白质解折叠的迹象)。CD光谱结果也证实了这种解折叠,并显示与氧化锌量子点接触的胰岛素的α螺旋含量降低,且其转变为无规卷曲。根据ITC结果,这种相互作用的ΔG、ΔH和结合常数分别为-32.35 kJ/mol、-43.21 kJ/mol和4.69×10⁵ M⁻¹。热聚集试验表明在氧化锌量子点存在的情况下胰岛素快速聚集。因此,在氧化锌量子点的生物医学应用如生物成像中,胰岛素附近存在此类量子点可能会使该蛋白质解折叠。

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