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.
Bianco
A
A
Centro di Studio sui Biopolimeri, Università di Padova, Italy.
Bertolini
T
T
Crisma
M
M
Valle
G
G
Toniolo
C
C
Maggini
M
M
Scorrano
G
G
Prato
M
M
D001426:Bacterial Proteins; D002244:Carbon / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D018360:Crystallography, X-Ray; D037741:Fullerenes; D047908:Intracellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D001426:Bacterial Proteins; D002352:Carrier Proteins; D037741:Fullerenes; D047908:Intracellular Signaling Peptides and Proteins; D010455:Peptides; C028640:fructose-induced HPr-like protein, bacteria; D002244:Carbon; D011392:Proline; C069837:fullerene C60