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Issue 32, 2007
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UV resonance Raman spectroscopic monitoring of supramolecular complex formation: peptide recognition in aqueous solution

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Abstract

The formation of a supramolecular complex between a tetrapeptide 2 and an artificial receptor 1, 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.

Graphical abstract: UV resonance Raman spectroscopic monitoring of supramolecular complex formation: peptide recognition in aqueous solution

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Publication details

The article was received on 15 Jun 2007, accepted on 12 Jul 2007 and first published on 27 Jul 2007


Article type: Paper
DOI: 10.1039/B709142G
Citation: Phys. Chem. Chem. Phys., 2007,9, 4598-4603
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    UV resonance Raman spectroscopic monitoring of supramolecular complex formation: peptide recognition in aqueous solution

    B. Küstner, C. Schmuck, P. Wich, C. Jehn, S. K. Srivastava and S. Schlücker, Phys. Chem. Chem. Phys., 2007, 9, 4598
    DOI: 10.1039/B709142G

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