Fig. 4: Aggregation kinetics of TEM and SHV proteins and peptides. | Nature Communications

Fig. 4: Aggregation kinetics of TEM and SHV proteins and peptides.

From: Exploiting the aggregation propensity of beta-lactamases to design inhibitors that induce enzyme misfolding

Fig. 4: Aggregation kinetics of TEM and SHV proteins and peptides.The alternative text for this image may have been generated using AI.

A Measurements of the hydrodynamic radius by Dynamic Light Scattering of 50 μM TEM3.2 in buffer alone, or in the presence of LPS or polyphosphate (PolyP). The data show a single representative replicate. B Amyloid-like aggregation kinetics of 50 μM TEM3.2 measured by Thioflavin-T (Th-T) fluorescence in the same conditions as A. Three replicates are shown for each condition. C Transmission Electron Micrograph of 50 μM TEM 3.2 incubated for 24 h in the same buffer as A with polyP, negatively stained with 2% (w/v) uranyl acetate. A single representative image is shown. D Amyloid-like aggregation kinetics of 50 μM TEM 3.2 in the PolyP condition in A, measured by pFTAA fluorescence. Three replicates are shown for each condition. E Aggregation kinetics using pFTAA fluorescence emission of recombinantly purified TEM-1, in the presence of vehicle, or TEM 3.2 peptin, as well as peptin-only control. F Similar as in E, but using an off-target Pept-In, based on an APR sequence of beta-galactosidase. G Similar to E, but now using a previously published off-target Pept-In, based on an APR of HcaB. The plots are the results of a single experiment, all replicates are shown. Source data are provided as a Source Data file.

Back to article page