Self-Assembling Lectin Nano-Block Oligomers Enhance Binding Avidity to Glycans

Irumagawa S, Hiemori K, Saito S, Tateno H, Arai R, International Journal of Molecular Sciences 23(2):676 (2022) DOI

SASDNC3 – Lectin nano-block dimer of WA20-SL-ACG

Lectin nano-block WA20-SL-ACG
MWI(0) 61 kDa
MWexpected 60 kDa
VPorod 82 nm3
log I(s) 1.30×10-1 1.30×10-2 1.30×10-3 1.30×10-4
Lectin nano-block WA20-SL-ACG small angle scattering data  s, nm-1
ln I(s)
Lectin nano-block WA20-SL-ACG Guinier plot ln 1.30×10-1 Rg: 3.1 nm 0 (3.1 nm)-2 s2
(sRg)2I(s)/I(0)
Lectin nano-block WA20-SL-ACG Kratky plot 1.104 0 √3 sRg
p(r)
Lectin nano-block WA20-SL-ACG pair distance distribution function Rg: 3.2 nm 0 Dmax: 14.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Lectin nano-block WA20-SL-ACG DAMMIN model
log I(s)
 s, nm-1
Lectin nano-block WA20-SL-ACG CORAL model
Synchrotron SAXS data from solutions of Lectin nano-block dimer of WA20-SL-ACG in 20 mM HEPES, 150 mM NaCl, 5% glycerol, pH 7.5 were collected on the BL-10C beam line at the Photon Factory (PF), High Energy Accelerator Research Organization (KEK; Tsukuba, Japan) using a Pilatus3 2M detector at a sample-detector distance of 2.1 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 3.54 mg/ml was measured at 20°C. 30 successive 5 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.

Artificial fusion protein of de novo protein WA20 and Agrocybe cylindracea galectin (ACG)

Lectin nano-block WA20-SL-ACG (WA20-SL-ACG)
Mol. type   Protein
Olig. state   Dimer
Mon. MW   30.0 kDa
Sequence   FASTA