β‐Turn induction by C60‐based fulleroproline: synthesis and conformational characterization of Fpr/Pro small peptides

Abstract
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 α‐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 H nuclear magnetic resonance, has been compared with the known propensity of the cognate‐l‐Pro‐d‐Ala‐sequence to adopt a βII‐turn conformation, which has also been confirmed in this work. The βII‐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. © Munksgaard 1997.

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