Hanatoxin

Hanatoxin is a toxin derived from the venom of the Tarantula species Grammostola spatulata. It is a member of the inhibitor cystine knot (ICK) family of peptides and is known for its ability to modulate voltage-gated potassium channels.

Structure[edit | edit source]

Hanatoxin is a 35-amino acid peptide with a unique structure. It contains an inhibitor cystine knot (ICK) motif, which is a characteristic feature of many spider toxins. This motif consists of a ring formed by two disulfide bonds and the intervening sections of the peptide backbone, with a third disulfide bond piercing through the center of the ring. This structure gives hanatoxin its stability and resistance to proteases.

Function[edit | edit source]

Hanatoxin modulates the function of voltage-gated potassium channels. It binds to these channels in the closed state and inhibits their opening, thereby affecting the flow of potassium ions across the cell membrane. This can affect the electrical activity of the cell, leading to effects such as paralysis in the organisms affected by the toxin.

Medical Significance[edit | edit source]

Research into hanatoxin and similar toxins could have significant implications for medicine. By studying how these toxins interact with ion channels, scientists can gain insights into the functioning of these channels in health and disease. This could potentially lead to the development of new drugs for conditions such as epilepsy, chronic pain, and cardiac arrhythmias.

References[edit | edit source]

Hanatoxin Resources
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