title: Metal ion complexation and folding of linear peptides.
abstract: A Linear peptide, GASYQDLG was synthesised and used as a model to evaluate the effects of nickel additions to increase the conformational stability. The NMR data obtained for the peptide and its histidyl derivative (H)(3)GASYQDLG(H)(3) suggest that in solution folded structures are present only for the H-tagged peptide-Ni(II) ion system. These results suggest that metal ions and additions of a double histidine tags of suitable length can be used as efficient tools to reduce peptide flexibility without other internal modifications. Synthesis of H-tagged analogs could offer a promising strategy for large-scale preparation of diagnostic tools and, in general, whenever more rigid molecular structures should be advisable.
authors.affiliation: Dipartimento di Biologia Molecolare, Centro per lo Studio Strutturale di Sistemi Biomolecolari, Via Fiorentina 1, 53100, Italy.
authors.forename: Ottavia
authors.initials: O
authors.lastname: Spiga
authors.forename: Maria
authors.initials: M
authors.lastname: Scarselli
authors.forename: Andrea
authors.initials: A
authors.lastname: Bernini
authors.forename: Arianna
authors.initials: A
authors.lastname: Ciutti
authors.forename: Leonardo
authors.initials: L
authors.lastname: Giovannoni
authors.forename: Franco
authors.initials: F
authors.lastname: Laschi
authors.forename: Luisa
authors.initials: L
authors.lastname: Bracci
authors.forename: Neri
authors.initials: N
authors.lastname: Niccolai
mesh_terms: D008670:Metals / Q000737:chemistry* / Q000378:metabolism; D009532:Nickel / Q000737:chemistry / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D008670:Metals; D009842:Oligopeptides; D009532:Nickel