Beta-turn induction by C60-based fulleroproline: synthesis and conformational characterization of Fpr/Pro small peptides.

We have recently described the preparation of Fpr (C60-based fulleroproline). In this paper the synthesis and a conformational characterization of heterochiral di- and tripeptides containing this new alpha-amino acid are reported. A folded structure, induced by the -L-Fpr-D-Ala-sequence in chloroform solution and detected by Fourier transform infrared absorption and 1H nuclear magnetic resonance, has been compared with the known propensity of the cognate -L-Pro-D-Ala-sequence to adopt a beta II-turn conformation, which has also been confirmed in this work. The beta II-turn structure is retained in the crystal state by the Pro-peptides, as shown by the X-ray diffraction structures of Ibu-L-Pro-D-Ala-NHtBu and Z-L-Pro-D-Ala-L-Ala-OtBu.