Extended Data Fig. 5: The high HSA binding affinity of proteins incorporated with lipidation mimics. | Nature Chemical Biology

Extended Data Fig. 5: The high HSA binding affinity of proteins incorporated with lipidation mimics.

From: Computational design and genetic incorporation of lipidation mimics in living cells

Extended Data Fig. 5

(a) Coomassie blue staining gel analysis of purified GLP-1 variants incorporated with indicated lipidation mimics. The experiment in the figure was repeated twice with similar results. (b) Mass spectrometry characterization of the fidelity of lipid mimics on GLP-1. The expected MW (-Met) of 4HexyF and 4OctyF incorporation were 15463 and 15491 Da, and the observed MW (-Met) were 15461 and 15490 Da, respectively. (c) MST analysis of affinity of GLP-1 variants for HSA. The data were fitted with Kd model by MO.Affinity analysis software and the binding affinity were shown. Error bars represented ± standard error of the mean (n = 3 biologically independent experiments). (d, e) ITC analysis of the affinity of GFP variants (D) or Neo-2/15 variants (E) for HSA. The data were fit to a single binding site model, and fitting thermostability parameters were shown in the figure.

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