阐明蛋白质吸附时界面水结构的变化。
Elucidating changes in interfacial water structure upon protein adsorption.
机构信息
Department of Chemistry, Texas A&M University, College Station, TX 77842-3012, USA.
出版信息
Chemphyschem. 2001 Sep 17;2(8-9):543-6. doi: 10.1002/1439-7641(20010917)2:8/9<543::AID-CPHC543>3.0.CO;2-5.
A coat to fit the body: Although protein adsorption onto surfaces is a complicated process, sum-frequency generation (SFG) spectroscopy probes the interfacial water structure around a silica surface as a model protein (bovine serum albumin, BSA) adsorbs onto it from solution. At pH 8.0, the attenuated SFG intensity after BSA adsorption indicates that interfacial water molecules are less ordered due to a reduction in surface ξ-potential. The SFG spectrum shows the C-O stretching vibrations subject to stronger ([symbol: see text]≈3200 cm(-1)) and weaker (3200 cm(-1)) hydrogen bonds.
贴合身体的外衣
尽管蛋白质在表面上的吸附是一个复杂的过程，但和频产生（SFG）光谱通过探测界面水结构来研究模型蛋白（牛血清白蛋白，BSA）从溶液中吸附到硅表面的过程。在 pH 值为 8.0 时，BSA 吸附后衰减的 SFG 强度表明由于表面ξ电势的降低，界面水分子的有序性降低。SFG 谱显示 C-O 伸缩振动受到较强（[符号：见正文]≈3200 cm(-1)) 和较弱（3200 cm(-1))氢键的影响。
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