Keywords: Cation, Peptide, Article, Circular Dichroism, Nonhuman, Nuclear Magnetic Resonance, Priority Journal, Amino Acid Sequence, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Molecular Structure, Protein Conformation,
Affiliations: Dipartimento di Chimica, Universita di Napoli, Via Mezzocannone 4, 80134 Napoli, Italy
References: Not available.
Stereochemical behavior of acyclic peptide-cation complexes
The role of the β-turns in the peptide interaction with several cations was investigated. In this work we report the solution studies of four linear peptides: Z-Aib-Aib-Aib-L-Val-OMe, Boc-D-aIle-L-Ile-D-aIle-L-Ile-OMe, Boc-L-Leu-D-Phe-Leu-L-Leu-L-Leu-OMe, and Boc-L-Phe-D-Phe-L-Phe-OMe. CD and 1H-nmr spectra reveal the presence of multiple ion-bonding equilibria. The stoichiometry and binding constant of the four peptides in the presence of Ca2+ ions in acetonitrile solution has been determined. Variable-temperature nmr spectra in the absence and in the presence of a large excess of cation have shown that the complexation process is not critically dependent on the conformation of the free peptide.
Stereochemical behavior of acyclic peptide-cation complexes
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