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The HMIQ3c1 recombinant peptide (6434 Da), the Kunitz-type protease inhibitor, which belonged to the new group of the IQ-peptides from the Heteractis magnifica sea anemone was prepared. The inhibitory constant of trypsin by this peptide proved to be 5.0 × 10-8 M. rHMIQ3c1 was shown to have no interaction with eight isoforms of Kv1 channels. This peptide exhibited neuroprotective activity in a concentration of 10 μM, and the peptide increased the viability of cells of the Neuro2a murine neuroblastoma by 39.4 ± 6.6% in the presence of β-amyloid. However, the peptide did not influence the viability of the cells during their incubation with 6-hydroxydofamine. [ABSTRACT FROM AUTHOR]

Antihistamine activity of recombinant peptides, Kunitz-type serine protease inhibitors of the sea anemone Heteractis crispa, was studied. It was shown that the peptides rHCGS1.19 and rHCGS1.36 at a concentration 10 μM inhibit an increase in the calcium ion concentration in macrophages elicited by histamine at 62.2 and 84.0%, respectively. The anti-inflammatory effect can be seen as the result of mediated reactions between peptides and proteases involved in these processes, as with the histamine H-type receptor blocking. [ABSTRACT FROM AUTHOR]