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, (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