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(Received for publication, May 18,
1995; and in revised form, August 3, 1995) New peptides have been isolated from the sea anemone Anemonia sulcata which inhibit competitively the binding of
Volume 270,
Number 42,
Issue of October 20, 1995 pp. 25121-25126
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
TWO DIFFERENT CLASSES OF SEA ANEMONE TOXINS FOR VOLTAGE-SENSITIVE
K CHANNELS
I-dendrotoxin I (a classical ligand for K
channel) to rat brain membranes and behave as blockers of
voltage-sensitive K
channels. Sea anemone kalicludines
are 58-59-amino acid peptides cross-linked with three disulfide
bridges. They are structurally homologous both to dendrotoxins which
are snake venom toxins and to the basic pancreatic trypsin inhibitor
(Kunitz inhibitor) and have the unique property of expressing both the
function of dendrotoxins in blocking voltage-sensitive K
channels and the function of the Kunitz inhibitor in inhibiting
trypsin. Kaliseptine is another structural class of peptide comprising
36 amino acids with no sequence homology with kalicludines or with
dendrotoxins. In spite of this structural difference, it binds to the
same receptor site as dendrotoxin and kalicludines and is as efficient
as a K
channel inhibitor as the most potent
kalicludine.
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