Cation channel formed at lipid bilayer by Cinnamomin, a new type II ribosome-inactivating protein
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Updated: Oct 19, 2026

Method for Identifying Small Molecule Inhibitors of the Protein-protein Interaction Between HCN1 and TRIP8b
Published on: November 11, 2016
1Shanghai Institute of Physiology, Chinese Academy of Sciences, People's Republic of China.
Abstract:
Cinnamomin, a new type II ribosome-inactivating protein, purified from the seeds of Cinnamonum camphora is reconstituted into the membranes of planar lipid bilayer and giant liposome. The channel-forming activity of the cinnamomin is found and cation permeability of the channel is characterized by patch clamp. In an asymmetric solution system, bath 150/pipette 100 mM KCl, the unit conductance is 140+/-7 pS and the reversal potential is 10.4+/-0.6 mV, very close to the theoretical value of the K+ electrode. The results offer an interpretation for internalization of the RIP and the cytotoxicity difference between single and two chain RIP.
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