Abstract
Abstract Conformational analysis of human proinsulin C-peptide fragments bound to cross-linked and soluble polystyrene resin matrices was performed using IR absorption spectroscopy. The conformational analysis of octa- and tridecapeptides in the swollen and solid states revealed that both peptides easily interacted with each other through intermolecular hydrogen bonding to form a β-sheet aggregation even at a low loading of peptide chains on the matrices. The high potential of the resin-bound peptides for the β-sheet formation was compatible with that of the corresponding peptides free from macromolecular protecting groups and was predicted using the average coil conformational value, 〈Pc〉, of each peptide. The significance of the results is discussed in connection with solid-phase peptide synthesis. Effects of shear stress on conformational transformations of resin-bound peptides was also examined in the solid state.
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