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

SASDVQ4 – Immunoglobulin light chain M10

Immunoglobulin light chain M10
MWexperimental 45 kDa
MWexpected 45 kDa
VPorod 58 nm3
log I(s) 2.67×101 2.67×100 2.67×10-1 2.67×10-2
Immunoglobulin light chain M10 small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin light chain M10 Guinier plot ln 2.67×101 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin light chain M10 Kratky plot 1.104 0 √3 sRg
p(r)
Immunoglobulin light chain M10 pair distance distribution function Rg: 2.6 nm 0 Dmax: 8.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Immunoglobulin light chain M10 ALPHAFOLD model
Synchrotron SAXS data from solutions of immunoglobulin light chain M10 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 2.8 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 M10 (M10)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   22.7 kDa
Sequence   FASTA