Adsorption of the cysteine-tryptophan dipeptide at the Au(110)/liquid interface studied using reflection anisotropy spectroscopy
Adsorption of the cysteine-tryptophan dipeptide at the Au(110)/liquid interface studied using reflection anisotropy spectroscopy
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DOI：
10.1016/j.susc.2010.09.010
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发表时间：
2010-11-01
期刊：
影响因子：
1.9
通讯作者：
Weightman, P.
中科院分区：
文献类型：
--
作者：
della Rocca, B. Morozzo;Smith, C. I.;Weightman, P.
的吸附cysteine-tryptophan dipepticle一直在监视一个非盟(110)/电解质界面使用反射各向异性光谱学在0 6 V二肽吸附通过形成Au-S债券和氨基之间的联系组非盟表面应用潜力是06年改为+ V氨基集团离开表面和光谱表明,两个二肽形成二硫桥与非盟结合表面这一事件伴随着取向的变化将外加电位恢复到06 V时，未能重建Au-S键的初始居群，并且在一小时的时间尺度上，正电位在色氨酸s相关光谱区域引起的变化是永久性的。色氨酸部分的细微变化表明，色氨酸的取向对外加电位非常敏感，电位的循环表现出稳定在低扫描速率下，Au-S键和au -二硫化键之间的相互转换，但在高扫描速率下，并非所有断裂的二硫化键都能够重新形成，在电位循环过程中，色氨酸区域也观察到不可逆的变化(C) 2010 Elsevier B V all rights reserved
The adsorption of a cysteine-tryptophan dipepticle has been monitored at a Au(110)/electrolyte interface using reflection anisotropy spectroscopy At -0 6 V the dipeptide adsorbed through the formation of Au-S bonds and a link between the NH2 group at the Au surface As the applied potential was changed to +06 V the NH2 group left the surface and the spectra suggest that two dipeptides form a disulphide bridge that binds to the Au surface This event is accompanied by changes in the orientation of and possibly interactions between tryptophan moieties Returning the applied potential to 06 V failed to re-establish the initial population of Au-S bonds and the changes induced in the region of the spectrum associated with the tryptophan s by the positive potentials were permanent on the time scale of an hour Subtle changes associated with the tryptophan moieties indicate that the orientation of the tryptophans is very sensitive to the applied potential Cycling of the potential showed a stable inter-conversion between Au-S bonds and Au-disulphide bonds at low scan rates but at higher scan rates not all the broken disulphide bonds were able to reform Irreversible changes were also observed in the tryptophan region of the spectrum during potential cycling (C) 2010 Elsevier B V All rights reserved