Obtaining AFM and TEM images of peptide fibres required dilution of the hydrogels. The cryoSEM technique provides a possibility to see the undiluted microstructures of the hydrogels. Previously registered cryoSEM images of RADA16-I were acquired from an aqueous dispersion of lyophilized powder . This technique revealed the porous morphology of the hybrids. This observation is in agreement with many other reported hydrogels, such as cellulosic super absorbent , freeze-dried agarose scaffolds , or collagen/chitosan scaffolds . No alveolar pattern was observed, which is typical for ice artefacts in cryoSEM . To our knowledge, these images are the first registered cryoSEM pictures for the RADA16-I hydrogel. The photographs of the RADA hybrids differ from unmodified RADA16-I in their characteristic branches inside the structures. These differences in morphology may be explained by parts of hydrogel not being cross-linked by normal interactions present in RADA peptides. It is probable that IM, GHK and KGHK, along with the glycine linkers and enzymatic sequence fragments, caused chunks of unfolded peptides and the occurrence of these ramifications. To prove that, there is a need to analyze differently modified RADA16-I peptides which can form hydrogels, by cryoSEM techniques, as well as ones which are a mixture of RADA16-I and an active sequence.