title: UV resonance Raman spectroscopic monitoring of supramolecular complex formation: peptide recognition in aqueous solution.
abstract: 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.
authors: Institut für Physikalische Chemie, Universität Würzburg, Am Hubland, 97074, Würzburg, Germany.
authors: Bernd
authors: B
authors: Küstner
authors: Carsten
authors: C
authors: Schmuck
authors: Peter
authors: P
authors: Wich
authors: Carina
authors: C
authors: Jehn
authors: Sunil K
authors: SK
authors: Srivastava
authors: Sebastian
authors: S
authors: Schlücker
mesh_terms: D001665:Binding Sites; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D018000:Receptors, Peptide / Q000737:chemistry; D013059:Spectrum Analysis, Raman; D014732:Vibration; D014867:Water / Q000737:chemistry*
chemical_list: D009842:Oligopeptides; D010455:Peptides; D018000:Receptors, Peptide; D014867:Water