Tertiapin

M.W. 2455.1

C₁₀₆H₁₇₆N₃₄O₂₃S₅

Ala- Leu- Cys- Asn- Cys- Asn- Arg- Ile- Ile- Ile- Pro- His- Met- Cys- Trp- Lys- Lys- Cys- Gly- Lys- Lys- NH2

Tertiapin, a high-affinity inhibitor for inward-rectifier K+ channels Tertiapin, a 21 amino acid residue peptide was originally isolated from honey bee venom and has been described recently as a novel K+ channel blocker. Tertiapin blocks a G protein-gated channel (GIRK1/4) and the ROMK1 channel with nanomolar affinity. About selectivity, tertiapin is insensitive to IRK1-channel, a closely related channel to GIRK1/4 and the ROMK1. Tertiapin will be a very useful tool for studying the physiological and the structure-function relationship of these channels. Inward-rectifier K+ channels accomplish many important and diversified biological roles. Thus far, there are no high-affinity inhibitors that directly target any inward-rectifier K+ channels. Only Lq2, scorpion toxin, blocks the ROMK1 inward-rectifier K+ channel, but the affinity is rather low (Kd = 0.4 mM) [Biochemistry, 36, 6936 (1997)].

Synthetic Product (disulfide bonds between Cys3– Cys14 and Cys5– Cys18 )

The purity is guaranteed to be higher than 99% by HPLC