Related Experiment Video
Updated: Jan 19, 2026
Identification of Hemolytic and Phospholipase Activity in Crude Extracts from Sea Anemones by Straightforward Bioassays
Published on: March 29, 2022
New Targets of Kunitz-Type Peptide from Sea Anemone Heteractis magnifica
A N Kvetkina1, L A Kaluzhskiy2, E V Leychenko3,4
1Elyakov Pacific Institute of Bioorganic Chemistry, Far East Branch, Russian Academy of Sciences, 690022, Vladivostok, Russia. kvetkinaan@gmail.com.
Abstract:
The interaction of Kunitz-type peptide, HMIQ3c1, from the sea anemone Heteractis magnifica with several serine proteases, including inflammatory proteases, was investigated using the surface plasmon resonance approach. We showed that the recombinant analog of HMIQ3c1 forms sufficiently strong complexes with trypsin (KD = 1.07 × 10-9 М) and chymotrypsin (KD = 4.70 × 10-8 М). Analysis of thermodynamic parameters of HMIQ3c1/chymotrypsin revealed significant contribution of the entropic factor to the complex formation. The formation of specific complexes of HMIQ3c1 with the kallikrein (KD = 2.81 × 10-8 М) and neutrophil elastase (KD = 1.11 × 10-7 М) indicates its anti-inflammatory activity and makes prospects to use the peptide as a potential therapeutic agent.
More Related Videos
10:46A Calcium Bioluminescence Assay for Functional Analysis of Mosquito Aedes aegypti and Tick Rhipicephalus microplus G Protein-coupled Receptors
Published on: April 20, 2011
08:09Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017