Fig. 6: Design and characterization of chimeric Fcs. | Nature Communications

Fig. 6: Design and characterization of chimeric Fcs.

From: The structure of the teleost Immunoglobulin M core provides insights on polymeric antibody evolution, assembly, and function

Fig. 6

a Top, the design of chimeric Fc constructs; bottom, schematic showing topology of chimeric Fc constructs. Each chimeric Fc consists of an N-terminal hexa-histidine tag, partial hFc sequence (orange), and tFcµ C-terminal sequence (marine or light blue). b–d SEC-MALS chromatograms for the indicated chimeric Fcs (top) and associated control complexes (bottom). SEC elution profiles are shown as solid curves (left axis; normalized UV signal) and light scattering data, indicating protein mass, is shown as horizontal dots (right axis; protein mass in kDa). All data are colored according to the key below. In top panels, average protein mass of controls is indicated by horizontal dashed lines. b hFcµ-tFcµ chimeric Fcs and relevant controls. c hFcα-tFcµ chimeric Fcs and relevant controls. d hFcγ1-tFcµ chimeric Fcs and relevant controls. For all samples, the predicted molecular weight from the protein sequence, the average molecular weight determined by MALS, and the number and potential of PNGS are listed in Supplementary Table 4. The amino acid sequences of chimeric Fc used in this study are provided in Supplementary Table 5. Source data are provided as a Source Data file.

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