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A Helical Peptide Receptor for [60]Fullerene
Author(s) -
Bianco Alberto,
Corvaja Carlo,
Crisma Marco,
Guldi Dirk M.,
Maggini Michele,
Sartori Elena,
Toniolo Claudio
Publication year - 2002
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20020402)8:7<1544::aid-chem1544>3.0.co;2-t
Subject(s) - peptide , crystallography , chemistry , fullerene , helix (gastropod) , side chain , stereochemistry , crystal structure , organic chemistry , ecology , biochemistry , snail , biology , polymer
Two terminally blocked 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 by solution methods and fully characterized. FT‐IR absorption and two‐dimensional NMR analyses indicate that a 3 10 ‐helical conformation is adopted by these rigid peptides in structure‐supporting solvents. An X‐ray diffraction investigation shows that the bis‐ L ‐Tyr(Me) nonapeptide in the crystal state is folded in a regular right‐handed 3 10 ‐helical structure. As five amino acid units separate the two substituted L ‐Tyr residues in the peptide sequence, the two side chain moieties will—in solution—face each other after two complete turns of the ternary helix. By carrying out a detailed photophysical analysis, we have demonstrated that the electron‐rich, hydrophobic and wide cavity generated by the nonapeptide template with two ferrocenoyloxybenzyl walls is able to host [60]fullerene. Further evidence for this superstructure has been provided in the gas phase by a mass spectrometric investigation.