Peptide Foldamers as Building Blocks for Ordered Nanomolecular Architectures

摘要: The determination of the structural features ordered, sterically constrained peptides (foldamers) in solution, membrane phase and supported onto appropriate surfaces can be performed making use a technique less powerful but cheaper than NMR, having high potentiality. This method combines results time-resolved FRET (fluorescence resonance energy transfer) measurements with those molecular mechanics calculations. Once structure main chain has been evaluated by other spectroscopic techniques, such as IR CD, deepest minimum conformers obtained mechanics, so that theoretical interprobe distance orientation their relative population compared fluorescence experiments. Where comparison between calculated measured quantities is successful, good piece information obtained, otherwise experimental used constraints for By applying this to number or bioactive pseudopeptides solution (mainly methanol water/methanol) model membranes (liposomes), we were able determine, degree confidence, structure. Some these structures later confirmed X-ray diffraction data solid state. application some presented discussed.