During the development of selective peptides against highly homologous targets, a reliable
tool is sought that can predict information on both mechanisms of binding and relative …

Potassium channel inhibitor peptides from scorpion venom, α-KTx, have greatly advanced
our understanding of potassium channel structure and function, Because of their high affinity …

Voltage-gated potassium channels (KV s) perform vital physiological functions and are
targets in different disorders ranging from ataxia and arrhythmia to autoimmune diseases …

Peptide toxins are potent and often exquisitely selective probes of the structure and function
of ion channels and receptors, and are therefore of significant interest to the pharmaceutical …

Abstract The voltage-gated Kv1. 3 K+ channel plays a key role in the activation of T
lymphocytes. Kv1. 3 blockers selectively suppress immune responses mediated by effector …

Voltage-dependent ion channels are a difficult class of proteins to approach biochemically.
Many such channels are present at low density in relevant tissues and exist as multiple …

This article reports the solution structure of BmTx3B (α‐KTx16. 2), a potassium channel
blocker belonging to the subfamily α‐KTx16, purified from the venom of the Chinese …

The bacterial potassium channel, KcsA, can be modified to express a high-affinity receptor
site for the scorpion toxin kaliotoxin (KTX) by substituting subregion I in the P region of KcsA …

Peptides that bind to ion channels have attracted much interest as potential lead molecules
for the development of new drugs and insecticides. However, the structure determination of …

Scorpion toxins interact with their target ion channels through multiple molecular contacts.
Because a “gain of function” approach has never been described to evaluate the importance …