短链聚乙二醇对人血清白蛋白周围水化结构及动力学的影响
Effect of Short Chain Poly(ethylene glycol)s on the Hydration Structure and Dynamics around Human Serum Albumin.
作者信息
Samanta Nirnay, Luong Trung Quan, Das Mahanta Debasish, Mitra Rajib Kumar, Havenith Martina
机构信息
Department of Chemical, Biological and Macromolecular Sciences, S.N. Bose National Centre for Basic Sciences , Block JD, Sector III, Salt Lake, Kolkata 700098, India.
Department of Physical Chemistry II, Ruhr-University Bochum , 44780 Bochum, Germany.
出版信息
Langmuir. 2016 Jan 26;32(3):831-7. doi: 10.1021/acs.langmuir.5b03884. Epub 2016 Jan 14.
We report the changes in the hydration dynamics around a globular protein, human serum albumin (HSA), in the presence of two short chain crowding agents, namely poly(ethylene glycol)s (PEG 200 and 400). The change in the network water structure is investigated using FTIR spectroscopy in the far-infrared (FIR) frequency range. Site specific changes are obtained by time-resolved fluorescence spectroscopic technique using the intrinsic fluorophore tryptophan (Trp214) of HSA. The collective hydration dynamics of HSA in the presence of PEG molecules are obtained using terahertz (THz) time domain spectroscopy (TTDS) and high intensity p-Ge THz measurements. Our study affirms a considerable perturbation of HSA hydration beyond a critical concentration of PEG.
我们报告了在两种短链拥挤剂，即聚乙二醇（PEG 200和PEG 400）存在的情况下，球状蛋白人血清白蛋白（HSA）周围水合动力学的变化。利用远红外（FIR）频率范围内的傅里叶变换红外光谱（FTIR）研究了网络水结构的变化。使用HSA的内在荧光团色氨酸（Trp214），通过时间分辨荧光光谱技术获得位点特异性变化。利用太赫兹（THz）时域光谱（TTDS）和高强度p-Ge太赫兹测量，获得了PEG分子存在下HSA的集体水合动力学。我们的研究证实，在PEG的临界浓度以上，HSA水合受到相当大的扰动。
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