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001-es BibID:	BIBFORM103838
035-os BibID:	(scopus)85132050297 (cikkazonosító)e202213146
Első szerző:	Naseem, Muhammad Umair (biofizikus, molekuláris biológus)
Cím:	Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity / Naseem Muhammad Umair, Carcamo-Noriega Edson, Beltrán-Vidal José, Borrego Jesus, Szanto Tibor G., Zamudio Fernando Z., Delgado-Prudencio Gustavo, Possani Lourival D., Panyi Gyorgy
Dátum:	2022
ISSN:	0022-1295 1540-7748
Megjegyzések:	The Cm28 in the venom of Centruroides margaritatus is a short peptide consisting of 27 amino acid residues with a mol wt of 2,820 D. Cm28 has <40% similarity with other known ?-KTx from scorpions and lacks the typical functional dyad (lysine?tyrosine) required to block KV channels. However, its unique sequence contains the three disulfide-bond traits of the ?-KTx scorpion toxin family. We propose that Cm28 is the first example of a new subfamily of ?-KTxs, registered with the systematic number ?-KTx32.1. Cm28 inhibited voltage-gated K+ channels KV1.2 and KV1.3 with Kd values of 0.96 and 1.3 nM, respectively. There was no significant shift in the conductance?voltage (G-V) relationship for any of the channels in the presence of toxin. Toxin binding kinetics showed that the association and dissociation rates are consistent with a bimolecular interaction between the peptide and the channel. Based on these, we conclude that Cm28 is not a gating modifier but rather a pore blocker. In a selectivity assay, Cm28 at 150 nM concentration (>100? Kd value for KV1.3) did not inhibit KV1.5, KV11.1, KCa1.1, and KCa3.1 K+ channels; NaV1.5 and NaV1.4 Na+ channels; or the hHV1 H+ channel but blocked ?27% of the KV1.1 current. In a biological functional assay, Cm28 strongly inhibited the expression of the activation markers interleukin-2 receptor and CD40 ligand in anti-CD3?activated human CD4+ effector memory T lymphocytes. Cm28, due to its unique structure, may serve as a template for the generation of novel peptides targeting KV1.3 in autoimmune diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk KV1.2 KV1.3 scorpion toxin
Megjelenés:	Journal Of General Physiology. - 154 : 8 (2022), p. 1-18. -
További szerzők:	Carcamo-Noriega, Edson Beltrán-Vidal, José Borrego, Jesús Szántó Gábor Tibor (1980-) (vegyész) Zamudio, Fernando Z. Delgado-Prudencio, Gustavo Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	K143071 OTKA K142612 OTKA K132906 OTKA CONACYT 303045 Egyéb Tempus Public Foundation Egyéb
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001-es BibID:	BIBFORM114858
035-os BibID:	(cikkazonosító)506 (scopus)85168734722 (wos)001056214900001
Első szerző:	Shakeel, Kashmala
Cím:	Of Seven New K⁺ Channel Inhibitor Peptides of Centruroides bonito, α-KTx 2.24 Has a Picomolar Affinity for Kv1.2 / Shakeel Kashmala, Olamendi-Portugal Timoteo, Naseem Muhammad Umair, Becerril Baltazar, Zamudio Fernando Z., Delgado-Prudencio Gustavo, Possani Lourival Domingos, Panyi Gyorgy
Dátum:	2023
ISSN:	2072-6651
Megjegyzések:	Seven new peptides denominated CboK1 to CboK7 were isolated from the venom of the Mexican scorpion Centruroides bonito and their primary structures were determined. The molecular weights ranged between 3760.4 Da and 4357.9 Da, containing 32 to 39 amino acid residues with three putative disulfide bridges. The comparison of amino acid sequences with known potassium scorpion toxins (KTx) and phylogenetic analysis revealed that CboK1 (?-KTx 10.5) and CboK2 (?-KTx 10.6) belong to the ?-KTx 10.x subfamily, whereas CboK3 (?-KTx 2.22), CboK4 (?-KTx 2.23), CboK6 (?-KTx 2.21), and CboK7 (?-KTx 2.24) bear > 95% amino acid similarity with members of the ?-KTx 2.x subfamily, and CboK5 is identical to Ce3 toxin (?-KTx 2.10). Electrophysiological assays demonstrated that except CboK1, all six other peptides blocked the Kv1.2 channel with Kd values in the picomolar range (24?763 pM) and inhibited the Kv1.3 channel with comparatively less potency (Kd values between 20?171 nM). CboK3 and CboK4 inhibited less than 10% and CboK7 inhibited about 42% of Kv1.1 currents at 100 nM concentration. Among all, CboK7 showed out-standing affinity for Kv1.2 (Kd = 24 pM), as well as high selectivity over Kv1.3 (850-fold) and Kv1.1 (~6000-fold). These characteristics of CboK7 may provide a framework for developing tools to treat Kv1.2-related channelopathies.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk CboK Centruroides bonito scorpion toxin Kv1.2 Kv1.3 Kv1.2 channelopathies electrophysiology
Megjelenés:	Toxins. - 15 : 8 (2023), p. 1-20. -
További szerzők:	Olamendi-Portugal, Timoteo Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Becerril, Baltazar Zamudio, Fernando Z. Delgado-Prudencio, Gustavo Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	K143071 OTKA
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