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. Author manuscript; available in PMC: 2019 Oct 23.
Published in final edited form as: ACS Nano. 2018 Aug 23;12(10):10130–10141. doi: 10.1021/acsnano.8b04947

Figure 2. Isothermal titration calorimetry (ITC) study of protein binding on NPs.

Figure 2.

The dynamic topographical structure of PEG shell reduces the affinity of protein binding on NPs. (a-d) Representative ITC data. Graphs show integrated heat of each titration (■) with a corresponding fitted curve based on the one-site binding model for (a) PLGA-NPs, (b) PLGA-PEG-NPs, (c) PLGA-TPEG-NP-20, and (d) PLGA-TPEG-NP-100. (e,f), Calculated stoichiometry (Na) and binding affinity (Ka) for the indicated samples. Values indicate mean ± SD (n = 3). ***, P < 0.001.