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A new family of weak K + channel toxins (designated κ-KTx) with a novel “bi-helical” scaffold has recently been characterized from Heterometrus fulvipes (Scorpionidae) venom. Based on the presence of the minimum functional dyad (Y5 and K19), κ-hefutoxin-1 (κ-KTx1.1) was investigated and found to block Kv 1.2 (IC 50 ∼40μM) and Kv 1.3 (IC 50 ∼150μM) channels. In the present study,...
A challenge in opioid peptide chemistry and pharmacology is the possibility to develop novel peptides with peripheral selectivity. An enzymatically stable opioid peptide could involve an antidiarrheal effect. For this reason, we constrained the highly selective and potent tetrapeptide morphiceptin with a 6-atom bridge, resulting in a cyclic amide and an ester analogue, 2 and 3, respectively.Taking...
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