Metal ion complexation and folding of linear peptides.
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.
Spiga
Ottavia
O
Dipartimento di Biologia Molecolare, Centro per lo Studio Strutturale di Sistemi Biomolecolari, Via Fiorentina 1, 53100, Italy.
Scarselli
Maria
M
Bernini
Andrea
A
Ciutti
Arianna
A
Giovannoni
Leonardo
L
Laschi
Franco
F
Bracci
Luisa
L
Niccolai
Neri
N
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
D008670:Metals; D009842:Oligopeptides; D009532:Nickel