title: Conformational analysis of dolastatin 10: an NMR and theoretical approach.
abstract: A solution conformational analysis of dolastatin 10, a powerful antineoplastic agent, has been carried out by means of nmr techniques and theoretical calculations. 1H mono- and bidimensional nmr experiments, as well as 1H-13C heterocorrelated spectra, have been performed on CD2Cl2 solutions. The most interesting nmr data is a huge shielding of the aCH(25) proton of the Dov residue, suggesting the presence of an interaction between the N-terminal and the aromatic C-terminal ends of the molecule. The possibility of a head-to-tail intermolecular association having been discarded, the presence of a series of preferred folded conformation has been hypothesized. Conformational theoretical analysis supports the nmr hypothesis of a folded peptide-like molecule, and a series of possible conformers in good agreement with the experimental data have been analyzed.
authors.affiliation: Department of Chemistry, University of Naples, Italy.
authors.forename: E
authors.initials: E
authors.lastname: Benedetti
authors.forename: T
authors.initials: T
authors.lastname: Carlomagno
authors.forename: F
authors.initials: F
authors.lastname: Fraternali
authors.forename: Y
authors.initials: Y
authors.lastname: Hamada
authors.forename: K
authors.initials: K
authors.lastname: Hayashi
authors.forename: L
authors.initials: L
authors.lastname: Paolillo
authors.forename: T
authors.initials: T
authors.lastname: Shioiri
mesh_terms: D000595:Amino Acid Sequence; D000970:Antineoplastic Agents / Q000737:chemistry*; D047630:Depsipeptides; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D008962:Models, Theoretical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D000970:Antineoplastic Agents; D047630:Depsipeptides; D009842:Oligopeptides; C064570:dolastatin 10