Küstner Bernd, Schmuck Carsten, Wich Peter, Jehn Carina, Srivastava Sunil K, Schlücker Sebastian
Institut für Physikalische Chemie, Universität Würzburg, Am Hubland, 97074, Würzburg, Germany.
Phys Chem Chem Phys. 2007 Aug 28;9(32):4598-603. doi: 10.1039/b709142g. Epub 2007 Jul 27.
The formation of a supramolecular complex between a tetrapeptide and an artificial receptor , is monitored at submillimolar concentrations in water by UV resonance Raman spectroscopy. Using 275 nm excitation, we selectively probe the carboxylate binding site (CBS) within the receptor, a moiety which is very efficient in binding the carboxy terminus of peptides in aqueous media. Complexation of the receptor with the tetrapeptide involves the formation of a H-bond enforced ion pair, resulting in significant changes in the corresponding UV resonance Raman spectra. Our qualitative interpretation is based on experimental reference and calculated Raman spectra on model systems. First preliminary calculations show that for a quantitative analysis, also the distinct contributions of multiple CBS conformers must be considered in addition to the H-bond induced changes upon complexation.
通过紫外共振拉曼光谱在水中亚毫摩尔浓度下监测四肽与人工受体之间超分子复合物的形成。使用275 nm激发，我们选择性地探测受体中的羧酸盐结合位点（CBS），该部分在水性介质中结合肽的羧基末端非常有效。受体与四肽的络合涉及形成氢键增强的离子对，导致相应的紫外共振拉曼光谱发生显著变化。我们的定性解释基于模型系统的实验参考和计算拉曼光谱。初步计算表明，为了进行定量分析，除了络合时氢键诱导的变化外，还必须考虑多个CBS构象体的不同贡献。
