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Tertiapin-Q

Tertiapin Q is a stable derivative of the bee venom toxin tertiapin. It is a high affinity blocker for inward-rectifier K+ channels that binds to ROMK1 (Kir1.1) and GIRK1/4 (Kir3.1/3.4) channels with high affinity (Ki values are 1.3 and 13.3 nM respectively).

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Tertiapin-Q(CAS 910044-56-3)

CAT No: R1101

CAS No:910044-56-3

Synonyms/Alias:910044-56-3;TPN(Q);AKOS024456523;

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cGMP Peptide
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M.F/Formula
C106H175N35O24S4
M.W/Mr.
2452
Sequence
One Letter Code:ALCNCNRIIIPHQCWKKCGKK
Three Letter Code:H-Ala-Leu-Cys(1)-Asn-Cys(2)-Asn-Arg-Ile-Ile-Ile-Pro-His-Gln-Cys(1)-Trp-Lys-Lys-Cys(2)-Gly-Lys-Lys-NH2
Labeling Target
Potassium channel
Appearance
White lyophilised solid
Activity
Blocker
Source#
Synthetic
Long-term Storage Conditions
Soluble in DMSO
InChI
InChI=1S/C106H175N35O24S4/c1-10-55(6)83-103(163)139-84(56(7)11-2)104(164)140-85(57(8)12-3)105(165)141-40-24-32-78(141)102(162)133-71(43-60-47-118-53-122-60)96(156)128-68(33-34-79(112)142)92(152)135-75-50-168-169-51-76(136-94(154)69(41-54(4)5)129-87(147)58(9)111)100(160)132-73(45-81(114)144)98(158)137-77(101(161)131-72(44-80(113)143)97(157)127-67(93(153)138-83)31-23-39-119-106(116)117)52-167-166-49-74(88(148)121-48-82(145)123-64(28-16-20-36-108)89(149)124-63(86(115)146)27-15-19-35-107)134-91(151)66(30-18-22-38-110)125-90(150)65(29-17-21-37-109)126-95(155)70(130-99(75)159)42-59-46-120-62-26-14-13-25-61(59)62/h13-14,25-26,46-47,53-58,63-78,83-85,120H,10-12,15-24,27-45,48-52,107-111H2,1-9H3,(H2,112,142)(H2,113,143)(H2,114,144)(H2,115,146)(H,118,122)(H,121,148)(H,123,145)(H,124,149)(H,125,150)(H,126,155)(H,127,157)(H,128,156)(H,129,147)(H,130,159)(H,131,161)(H,132,160)(H,133,162)(H,134,151)(H,135,152)(H,136,154)(H,137,158)(H,138,153)(H,139,163)(H,140,164)(H4,116,117,119)/t55-,56-,57-,58-,63-,64-,65-,66-,67-,68-,69-,70-,71-,72-,73-,74-,75-,76-,77-,78-,83-,84-,85-/m0/s1
InChI Key
GMZAXHIZSCRCHM-MIPBWYARSA-N
Isomeric SMILES
CC[C@H](C)[C@H]1C(=O)N[C@H](C(=O)N[C@H](C(=O)N2CCC[C@H]2C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@H]3CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@@H](NC3=O)CC4=CNC5=CC=CC=C54)CCCCN)CCCCN)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N)C(=O)N[C@H](C(=O)N[C@H](C(=O)N1)CCCNC(=N)N)CC(=O)N)CC(=O)N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)N)CCC(=O)N)CC6=CNC=N6)[C@@H](C)CC)[C@@H](C)CC
BoilingPoint
N/A
References

The stability of TPNQ allows us to investigate how it interacts with the targeted channels. We found that the interaction between TPNQ and the ROMK1 channel is a bimolecular reaction, i.e., one TPNQ molecule binds to one channel. The interaction surface in TPNQ is primarily formed by its α helix rather than the β sheets with which scorpion toxins form their interaction surface. The mutagenesis studies on both the channel and TPNQ together strongly suggest that to block the K+pore TPNQ plugs its α helix into the vestibule of the K+ pore, while leaving the extended structural portion sticking out of the vestibule into the extracellular media.

Mechanisms of Inward-Rectifier K+ Channel Inhibition by Tertiapin-Q

Melting Point
N/A

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