A conformational fingerprint for amyloidogenic light chains

Paissoni C, Puri S, Broggini L, Sriramoju M, Maritan M, Russo R, Speranzini V, Ballabio F Nuvolone M, Merlini G, Palladini G, Hsu S, Ricagno S, Camilloni C, eLife 13 (2025) DOI

SASDVN4 – Immunoglobulin light chain H18

Immunoglobulin light chain H18
MWexperimental 43 kDa
MWexpected 43 kDa
VPorod 58 nm3
log I(s) 1.97×101 1.97×100 1.97×10-1 1.97×10-2
Immunoglobulin light chain H18 small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin light chain H18 Guinier plot ln 1.97×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin light chain H18 Kratky plot 1.104 0 √3 sRg
p(r)
Immunoglobulin light chain H18 pair distance distribution function Rg: 2.6 nm 0 Dmax: 8.2 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Immunoglobulin light chain H18 SWISSMODEL model
Synchrotron SAXS data from solutions of immunoglobulin light chain H18 in 20 mM TrisHCL, 150 mM NaCl, pH 8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus3 2M detector at a sample-detector distance of 3.0 m and at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 100.00 μl sample at 6.7 mg/ml was injected at a 0.10 ml/min flow rate onto a Cytiva Superdex 200 Increase 10/300 column at 10°C. 1400 successive 2 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.

Immunoglobulin light chain H18 (H18)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   21.4 kDa
Sequence   FASTA