We proved that the synthesized peptides released the active motifs when treated with elastase, as designed. Mass spectrometry analysis confirmed that all hybrid peptides were cleaved between Val and Gly immediately after the AAPV sequence (Fig. -fragments 1). In the case of RADA-IM, the digestion occurred after Gly, leaving the GGRDKVYR and GGGRDKVYR motif free. Some other fragments appeared on the RADA-KGHK mass spectrum, showing an additional aminoacids in cleaved fragmets ei. PV and APV, which is consistent with character of elastase cleaving peptides preferentially at the C-teminus of aliphatic aminoacids. Nevertheless, in all cases, fragments corresponding to the gelling fragment and the enzyme were identified. This concept, where an enzyme behaves as a triggering factor to release active motifs, has previously been reported .