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001-es BibID:	BIBFORM052924
Első szerző:	Bartók Ádám (biotechnológus)
Cím:	Margatoxin is a non-selective inhibitor of human Kv1.3 K+ channels / Adam Bartok, Agnes Toth, Sandor Somodi, Tibor G. Szanto, Peter Hajdu, Gyorgy Panyi, Zoltan Varga
Dátum:	2014
ISSN:	0041-0101
Megjegyzések:	Margatoxin (MgTx), an alpha-KTx scorpion toxin, is considered a selective inhibitor of the Kv1.3 K+ channel. This peptide is widely used in ion channel research; however, a comprehensive study of its selectivity with electrophysiological methods has not been published yet. The lack of selectivity might lead to undesired side effects upon therapeutic application or may lead to incorrect conclusion regarding the role of a particular ion channel in a physiological or pathophysiological response either in vitro or in vivo. Using the patch-clamp technique we characterized the selectivity profile of MgTx using L929 cells expressing mKv1.1 channels, human peripheral lymphocytes expressing Kv1.3 channels and transiently transfected tsA201 cells expressing hKv1.1, hKv1.2, hKv1.3, hKv1.4-IR, hKv1.5, hKv1.6, hKv1.7, rKv2.1, Shaker-IR, hERG, hKCa1.1, hKCa3.1 and hNav1.5 channels. MgTx is indeed a high affinity inhibitor of Kv1.3 (Kd = 11.7 pM) but is not selective, it inhibits the Kv1.2 channel with similar affinity (Kd = 6.4 pM) and Kv1.1 in the nanomolar range (Kd = 4.2 nM). Based on our comprehensive data MgTX has to be considered a non-selective Kv1.3 inhibitor, and thus, experiments aiming at elucidating the significance of Kv1.3 in in vitro or in vivo physiological responses have to be carefully evaluated.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban ion channel potassium channel scorpion toxin margatoxin
Megjelenés:	Toxicon. - 87 (2014), p. 6-16. -
További szerzők:	Tóth Ágnes (1983-) (biofizikus) Somodi Sándor (1977-) (belgyógyász) Szántó Gábor Tibor (1980-) (vegyész) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
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001-es BibID:	BIBFORM063758
Első szerző:	Olamendi-Portugal, Timoteo
Cím:	Isolation, chemical and functional characterization of several new K+-channel blocking peptides from the venom of the scorpion Centruroides tecomanus / Timoteo Olamendi-Portugal, Adam Bartok, Fernando Zamudio-Zuniga, Andras Balajthy, Baltazar Becerril, Gyorgy Panyi, Lourival D. Possani
Dátum:	2016
ISSN:	0041-0101
Megjegyzések:	AbstractSix new peptides were isolated from the venom of the Mexican scorpion Centruroides tecomanus; their primary structures were determined and the effects on ion channels were verified by patch-clamp experiments. Four are K(+)-channel blockers of the ?-KTx family, containing 32 to 39 amino acid residues, cross-linked by three disulfide bonds. They all block Kv1.2 in nanomolar concentrations and show various degree of selectivity over Kv1.1, Kv1.3, Shaker and KCa3.1 channels. One peptide has 42 amino acids cross-linked by four disulfides; it blocks ERG-channels and belongs to the ?-KTx family. The sixth peptide has only 32 amino acid residues, three disulfide bonds and has no effect on the ion-channels assayed. It also does not have antimicrobial activity. Systematic numbers were assigned (time of elution on HPLC): ?-KTx 10.4 (time 24.1); ?-KTx 2.15 (time 26.2); ?-KTx 2.16 (time 23.8); ?-KTx 2.17 (time 26.7) and ?-KTx 1.9 (elution time 29.6). A partial proteomic analysis of the short chain basic peptides of this venom, which elutes on carboxy-methyl-cellulose column fractionation, is included. The pharmacological properties of the peptides described in this study may provide valuable tools for understanding the structure-function relationship of K(+) channel blocking scorpion toxins.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Toxicon 115 (2016), p. 1-12. -
További szerzők:	Bartók Ádám (1984-) (biotechnológus) Zamudio, Fernando Z. Balajthy András (1988-) (általános orvos) Becerril, Baltazar Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
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