Two nonapeptides, each made up of six Aib residues, a Gly spacer and two L-Tyr residues in positions 2 and 8 (these are substituted in the side chain with either ferrocenoyl or methyl moieties) have been synthesized. Solution conformational analyses (FT-IR and NMR) indicate that a 3-10-helical conformation is adopted by these rigid peptides in strucutre-supporting solvents. An X-ray diffraction investigation shows that the bis-L-Tyr(Me) nonapeptide in the crystal state is folded into a regular right-handed 3-10-helical structure. A detailed photophysical analysis provides evidence that the electron-rich, hydrophobic and wide cavity generated by the nonapeptide with two ferrocenoylbenzyl walls is able to host [60]fullerene.
A helical peptide receptor for [60]fullerene
Crisma M;
2002
Abstract
Two nonapeptides, each made up of six Aib residues, a Gly spacer and two L-Tyr residues in positions 2 and 8 (these are substituted in the side chain with either ferrocenoyl or methyl moieties) have been synthesized. Solution conformational analyses (FT-IR and NMR) indicate that a 3-10-helical conformation is adopted by these rigid peptides in strucutre-supporting solvents. An X-ray diffraction investigation shows that the bis-L-Tyr(Me) nonapeptide in the crystal state is folded into a regular right-handed 3-10-helical structure. A detailed photophysical analysis provides evidence that the electron-rich, hydrophobic and wide cavity generated by the nonapeptide with two ferrocenoylbenzyl walls is able to host [60]fullerene.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
