Experiments to determine stability in plasma were conducted with diluted gels (0.1 mg/ml). These experiments aimed to assess if the peptides can be easily degraded and cleared from the wound site. Albumins can be responsible for the absence of RADA hybrids in plasma, which was shown in our experiments. Albumins are known to be good transporters , and all RADA hybrids have a strong affinity to them. It has previously been reported that RADA16-I scaffolds are biodegradable by various proteases and are thus biocompatible. The experiments proved that non-gelled hybrids are quickly eliminated. Due to their nature, they are probably hydrolyzed into amino acids. The quadruple Arg-Ala-Asp-Ala sequence is responsible for turning the peptide into a gel to stabilize the active sequence against enzymatic degradation and extend the release of the peptide by slowing down its degradation. Such strategies have been successfully applied previously . The decay occurs at the junction of two phases, namely gel and plasma. The gel is penetrated by the plasma over time, and is digested at a much slower pace than the non-gelled peptide.