IgG4 and IgG1 undergo common acid‐induced compaction into an alternatively folded state

Imamura H, Honda S, FEBS Letters (2025) DOI

SASDW44 – Immunoglobulin G4 (pH 2, 0.2 M NaCl), SEC-SAXS data

humanized immunoglobulin G4 monoclonal antibody (lebrikizumab)
MWI(0) 141 kDa
MWexpected 148 kDa
VPorod 238 nm3
log I(s) 1.02×10-1 1.02×10-2 1.02×10-3 1.02×10-4
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) small angle scattering data  s, nm-1
ln I(s)
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) Guinier plot ln 1.02×10-1 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) Kratky plot 1.104 0 3 sRg
p(r)
humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) pair distance distribution function Rg: 4.2 nm 0 Dmax: 14.0 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Immunoglobulin G4 in 100 mM glycine-HCl, 200 mM NaCl, pH 2 were collected on the BL-10C beam line at the Photon Factory High Energy Accelerator Research Organization (KEK; Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 1 m and at a wavelength of λ = 0.15 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 200.00 μl sample at 12.5 mg/ml was injected at a 0.20 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 25°C. Nine successive 20 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.

Relaibel minimum s is ~0.15 nm-1, approximated by a standard sample (lysozyme protein) scattering. DrugBank ID: DB11914: https://go.drugbank.com/drugs/DB11914

humanized immunoglobulin G4 monoclonal antibody (lebrikizumab) (IgG4)
Mol. type   Protein
Organism   Mouse/human
Olig. state   Monomer
Mon. MW   148 kDa
Sequence   FASTA