Fig. 5: Structural, biochemical and biophysical characterisation of the PenG-specific response. | Nature Communications

Fig. 5: Structural, biochemical and biophysical characterisation of the PenG-specific response.

From: Covalent penicillin-protein conjugates elicit anti-drug antibodies that are clonally and functionally restricted

Fig. 5

a Annotated chemical structure of PenG-lys construct used for uSTA analysis. b Saturation transfer difference spectrum was generated from the difference between the raw off-resonance (gaussian at 37 ppm) and the raw on-resonance (gaussian at 9 ppm) spectra. Data showing differences in para engagement in the benzene ring of MIL-2 fab versus MIL-1. c i. Heatmaps corresponding to saturation transfer efficiency of PenG-lys (1 mM) with MIL-1–3 (5 µM). ii. Histographic saturation transfer efficiencies. Red indicates high transfer efficiency. d SPR chip design. e Biophysical characterization of MIL-3 via SPR. f i. Top view of the x-ray structure of the MIL-3 Fab bound to the PenG-Lys (beige sticks). Both heavy (monochrome plum) and light chain (monochrome blue) CDRs are marked. Key residues within 4.0 Å of ligand aspects ii. phenylacetamide, iii. thiazolidine and iv. lysine are shown. Hydrogen bonds are shown as black broken lines. Water is marked in red. Source data are provided as a Source Data file.

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