Encapsulating additives including proteins in gels formed by LMWG is trivial. The proteins are trapped in the space between the fibers; if the gel network is sufficiently permanent and the pores between fibers sufficiently small, the protein is unable to easily diffuse within the gel and hence aggregate. Combining this concept with the potential for these gels to break at low strain means we can form gels within a syringe for long term room temperature storage, followed by release through a syringe filter; the essentially insoluble extended supramolecular network will be trapped within the syringe filter, meaning that only the pure protein is released (Fig. and). A model macromolecular cargo was loaded into gels to probe the impact on gel structure, function, and release. Dextran (Mr 6000 Da, hydrodynamic radius = 1.6 nm ) was chosen as a noninteracting additive with a similar size to insulin. Dextran was added at concentrations up to 10 wt% (Fig. , a value far above the loadings required for real-world drug storage and in line with recent moves towards higher concentration biologic formulations), whilst keeping all other parameters constant. Our gelation approach is almost instantaneous: in comparison, chemically triggered hydrogel storage solutions require addition of dosed release agents, such as sugars, and require up to an hour to gel. The gel properties were retained over all loadings, which is essential for a broadly applicable storage solution (Fig. ). Extended aging experiments showed that these properties did not change significantly over at least 136 days (Fig. ). The gels can be formed in situ inside a syringe. The added dextran does not affect the gelator's packing (Fig. ). As initial proof-of-concept, we entrapped a fluorescent dextran within a gel and then extruded through a syringe filter. Pure dextran was collected directly (Fig. ). No gelator could be detected in the extruded liquid by 1 H NMR spectroscopy (Fig. ), showing that the gel network is trapped within the syringe filter and our simple approach leads to excipient-free homogeneous protein on demand. The gelator is trapped in the filter as shown by FT-IR data (Fig. ). To add further quantification, we used LMWG which incorporate an inherently fluorescent group. After extrusion, very low fluorescence could be detected in the extrudates (< 5 ppm; Fig. ), showing the power of this approach (Fig. ). confirmation that macromolecules can be encapsulated and selectively released by mechanical trigger, protein storage was undertaken to demonstrate recovery and the mode of action (preventing aggregation). As a first challenge, we chose to encapsulate (bovine) insulin as a model therapeutic protein (Figure ). Insulin is one of the most widely used protein drugs in the world but must be stored cool or freeze-dried requiring the user to self-prepare the solution prior to injection. The instructions for insulin are very specific not to shake, as it is prone to aggregate into extended amyloid fibers losing efficacy and bioavailability. After initial screening using dynamic light scattering, insulin was loaded into gels (with no Ca 2+ in this case), which were then incubated at 25°C and shaken at 600 rpm: this is very aggressive agitation far beyond a real-world stress. After this, pure excipient-free protein was recovered by action of the syringe and any aggregation to amyloid was determined by the ThT (thioflavin T) assay, Figure . It should be noted, all samples were treated identically, and the solution-only samples were passed through the syringe filter, so there was no bias due to filter/exclusion of aggregates. Limited aggregation was detected in the gel loaded samples, but extensive aggregation occurred in the absence of the gel. In no case was gelator detected in the solutions extruded through the syringe filter. Hence, our approach provides dual protection against aggregation and allows protein release in a pure form. We tested two structurally related LMWG (Figure ) which also protected insulin against aggregation, confirming our mode of action linked to physical immobilization, not a specific interaction Insulin provided an aggregative readout, but it is also important to ensure (folded) protein function could be retained. Therefore, beta galactosidase (b-gal) was encapsulated (with added Ca 2+ ). b-Gal catalyzes the decomposition of p-nitrophenyl-galactoside allowing colorimetric evaluation of activity. The gels were placed in an incubator at 50°C (a stringent test beyond feasible transport conditions) for 7 days. After this time, protein was recovered by simple syringe action. Compared to fresh, b-gal in buffer alone retained just 26.1 ± 0.4 % of its function but across 15 repeats (3 technical, 5 biological) the gel-stored protein recovered 84.4 -108.1 % of function ((per protein mass), with a mean of 97.1 ± 2.8 %. This is equal performance to a novel multi-armed boronicacid function PEG hydrogel, 11 but our technology functions at biomedically relevant volumes (0.5 mL versus 50 µL), does not require addition of any triggers such as sugars or acid, and the resulting protein was excipient-free. As an even more challenging test, gels were stored at 50°C but for 4 weeks. This removed all activity from the solution-stored b-gal, but the gel-stored protein retained up to 20 % of its function: this is a remarkable level of recovery from a harsh storage condition at conditions that even the hottest locations on earth rarely face. To show the gels are robust, samples were mailed through the UK postal service to experience a realistic distribution challenge (shaking, dropping, temperature range; Fig. ). Over the 2 day delivery, the gels were recovered intact and ~ 100% activity was retained, showing that this method could conceptually be used for the postal delivery of active proteins for healthcare (Fig. ).