MMP-triggered nanogel disassembly was analysed using MMP-7 as a model MMP. We first confirmed that the free peptide in solution can be cleaved by MMP-7 as shown using LC-MS (Figure ). We next established the necessary concentrations of MMP-7 to successfully degrade the cross-links of the nanogels, which revealed that physiologically relevant nanomolar concentrations are sufficient for degradation (Figures S4). The kinetics of MMP-7responsive nanogel disassembly at a fixed enzyme concentration (90 nM) were subsequently studied by DLS (normalised derived count rate (in kcps) vs incubation time). The kinetic study (Figure ) reveals a drop in the scattering intensity over time only in the presence of the enzyme, indicating a decrease in nanogel concentration and/or size. The kcps value remained unvaried in the control nanogel sample without enzyme (red symbols). A further control, incubating the cross-linked nanogels at 37 °C in 5 % (v/v) fetal bovine serum (FBS) revealed very high stability of the nanogels in the presence of proteins over at least two days (Figure ). This confirms the ability of the nanogels to undergo enzyme-triggered degradation. From the evolution of scattering intensity in Figure it is apparent that degradation has already occurred to some extent after 1 h incubation with MMP-7. The number mean size of the nanogels has already decreased (measured below the LCST), which suggests the presence of differently sized fragments and partial degradation. Within the next few hours of incubation with enzyme, a mixture of differently sized particles/fragments/polymers (large errors) was detected. An equilibrium is reached after 24 h incubation, when a clear size difference between the control and enzyme incubated sample became apparent (Figure ).