Fig. 5: Enhanced catalytic efficiency and stability of P7 coacervates over time. | Nature Communications

Fig. 5: Enhanced catalytic efficiency and stability of P7 coacervates over time.

From: Catalytic peptide-based coacervates for enhanced function through structural organization and substrate specificity

Fig. 5: Enhanced catalytic efficiency and stability of P7 coacervates over time.

a Reaction scheme depicting the hydrolysis of p-nitrophenyl phosphate (pNPP) (b) kinetics of P7 peptide-based coacervates (in blue squares) and P7 in bulk solution (red dots) towards the substrate pNPP. The data fitting followed the Michaelis-Menten equation \(V0=V\max \left[S\right]/({KM})\). Data are presented as mean values ± SD (n = 3) from three independent experiments. In the bulky solution the errors bars are not visible (c) Representative confocal microscopy images showing stability of P7-based coacervates during the hydrolysis of pNPP, at 0 h vs 48 h. Source data are provided as a Source Data file (d), Reaction scheme illustrating the hydrolysis of 2´-[2-benzothiazoyl]−6´-hydroxybenzothiazole phosphate (BBTP). e Representative confocal images showing the progression of BBTP hydrolysis over time. f Percentage of coacervates that are fluorescent due to the formation of the BBT product during BBTP hydrolysis over time. Data are presented as mean values ± SD (n = 5) of five independent samples. Source data are provided as a Source Data file. All scale bars: 10 μm.

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