A tetracationic porphyrin with dual anti-prion activity.

Masone A, Zucchelli C, Caruso E, Lavigna G, Eraña H, Giachin G, Tapella L, Comerio L, Restelli E, Raimondi I, Elezgarai SR, De Leo F, Quilici G, Taiarol L, Oldrati M, Lorenzo NL, García-Martínez S, Cagnotto A, Lucchetti J, Gobbi M, Vanni I, Nonno R, Di Bari MA, Tully MD, Cecatiello V, Ciossani G, Pasqualato S, Van Anken E, Salmona M, Castilla J, Requena JR, Banfi S, Musco G, Chiesa R, iScience 26(9):107480 (2023) Europe PMC

SASDNB8 – Mature full length human prion protein

Major prion protein
MWexperimental 27 kDa
MWexpected 23 kDa
log I(s) 2.91×101 2.91×100 2.91×10-1 2.91×10-2
Major prion protein small angle scattering data  s, nm-1
ln I(s)
Major prion protein Guinier plot ln 2.91×101 Rg: 2.8 nm 0 (2.8 nm)-2 s2
(sRg)2I(s)/I(0)
Major prion protein Kratky plot 1.104 0 √3 sRg
p(r)
Major prion protein pair distance distribution function Rg: 2.9 nm 0 Dmax: 10.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Mature full length human prion protein Rg histogram Rg, nm
Major prion protein EOM/RANCH model
Synchrotron SAXS data from solutions of Mature full length human prion protein in 10 mM HEPES 100 mM NaCl, pH 7 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 20°C. 10 successive 0.500 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Major prion protein
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   22.8 kDa
 
UniProt   P04156 (23-231)
Sequence   FASTA