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001-es BibID:	BIBFORM102212
035-os BibID:	(cikkazonosító)115023 (WoS)000793623600002 (Scopus)85127510848
Első szerző:	Csóti Ágota (biológus)
Cím:	sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity / Csoti Agota, del Carmen Nájera Meza Rosby, Bogár Ferenc, Tajti Gabor, Szanto Tibor G., Varga Zoltan, Gurrola Georgina B., Tóth Gábor K., Possani Lourival D., Panyi Gyorgy
Dátum:	2022
ISSN:	0006-2952
Megjegyzések:	Kv1.3 K+ channels play a central role in the regulation of T cell activation and Ca2+ signaling under physiological and pathophysiological conditions. Peptide toxins targeting Kv1.3 have a significant therapeutic potential in the treatment of autoimmune diseases; thus, the discovery of new toxins is highly motivated. Based on the transcriptome analysis of the venom gland of V. mexicanus smithi a novel synthetic peptide, sVmKTx was generated, containing 36 amino acid residues. sVmKTx shows high sequence similarity to Vm24, a previously characterized peptide from the same species, but contains a Glu at position 32 as opposed to Lys32 in Vm24. Vm24 inhibits Kv1.3 with high affinity (Kd = 2.9 pM). However, it has limited selectivity (~1,500-fold) for Kv1.3 over hKv1.2, hKCa3.1, and mKv1.1. sVmKTx displays reduced Kv1.3 affinity (Kd = 770 pM) but increased selectivity for Kv1.3 over hKv1.2 (~9,000-fold) as compared to Vm24, other channels tested in the panel (hKCa3.1, hKv1.1, hKv1.4, hKv1.5, rKv2.1, hKv11.1, hKCa1.1, hNav1.5) were practically insensitive to the toxin at 2.5 ?M. Molecular dynamics simulations showed that introduction of a Glu instead of Lys at position 32 led to a decreased structural fluctuation of the N-terminal segment of sVmKTx, which may explain its increased selectivity for Kv1.3. sVmKTx at 100 nM concentration decreased the expression level of the Ca2+ -dependent T cell activation marker, CD40 ligand. The high affinity block of Kv1.3 and increased selectivity over the natural peptide makes sVmKTx a potential candidate for Kv1.3 blockade-mediated treatment of autoimmune diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Kv1.3 Toxin-channel interaction T-cell activation Patch-clamp Ion channel selectivity Scorpion toxin
Megjelenés:	Biochemical Pharmacology. - 199 (2022), p. 1-14. -
További szerzők:	del Carmen Nájera Meza, Rosby Bogár Ferenc Tajti Gábor (1988-) (gyógyszerész, biofizikus, sejtbiológus) Szántó Gábor Tibor (1980-) (vegyész) Varga Zoltán (1969-) (biofizikus, szakfordító) Gurrola-Briones, Georgina Tóth Gábor K. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	143071 OTKA K119417 OTKA K132906 OTKA EFOP-3.6.2-16-2017-00006 EFOP GINOP-2.3.2-15-2016-00044 GINOP PRONACE303045 from National Conseil of Science and Technology of Mexico Egyéb Ministry of Human Capacities, Hungary grant, TKP-2020 Egyéb
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001-es BibID:	BIBFORM044563
Első szerző:	Gurrola-Briones, Georgina
Cím:	Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24 : a novel potent blocker of Kv1.3 potassium channels of human T lymphocytes / Gurrola G. B., Hernandez-Lopez R. A., Rodriguez de la Vega R. C., Varga Z., Batista C. V., Salas-Castillo S. P., Panyi G., del Rio-Portilla Federico, Possani L. D.
Dátum:	2012
Megjegyzések:	Animal venoms are rich sources of ligands for studying ion channels and other pharmacological targets. Proteomic analyses of the soluble venom from the Mexican scorpion Vaejovis mexicanus smithi showed that it contains more than 200 different components. Among them, a 36-residue peptide with a molecular mass of 3864 Da (named Vm24) was shown to be a potent blocker of Kv1.3 of human lymphocytes (K(d) approximately 3 pM). The three-dimensional solution structure of Vm24 was determined by nuclear magnetic resonance, showing the peptide folds into a distorted cystine-stabilized alpha/beta motif consisting of a single-turn alpha-helix and a three-stranded antiparallel beta-sheet, stabilized by four disulfide bridges. The disulfide pairs are formed between Cys6 and Cys26, Cys12 and Cys31, Cys16 and Cys33, and Cys21 and Cys36. Sequence analyses identified Vm24 as the first example of a new subfamily of alpha-type K(+) channel blockers (systematic number alpha-KTx 23.1). Comparison with other Kv1.3 blockers isolated from scorpions suggests a number of structural features that could explain the remarkable affinity and specificity of Vm24 toward Kv1.3 channels of lymphocytes
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Amino Acid Motifs Animal Animals antagonists & inhibitors article chemical synthesis chemistry Disulfides drug effects Drug Evaluation,Preclinical Human Humans Ion Channels Kv1.3 Potassium Channel ligand Ligands lymphocyte Lymphocytes Magnetic Resonance Spectroscopy methods Mexico Mice Models,Molecular Peptides pharmacology Phylogeny Potassium Potassium Channel Blockers Potassium Channels Protein Conformation Research Research Support Scorpion Venoms Scorpions Support t lymphocyte T-Lymphocytes
Megjelenés:	Biochemistry 51 : 19 (2012), p. 4049-4061. -
További szerzők:	Hernandez-Lopez, Rogelio A. Rodriguez de la Vega, Ricardo C. Varga Zoltán (1969-) (biofizikus, szakfordító) Batista, Cesar V. F. Salas-Castillo, Saida P. Panyi György (1966-) (biofizikus) del Rio-Portilla, Federico Possani, Lourival Domingos
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001-es BibID:	BIBFORM106364
035-os BibID:	(cikkazonosító)41 (WoS)000916020800001 (Scopus)85146824862
Első szerző:	Naseem, Muhammad Umair (biofizikus, molekuláris biológus)
Cím:	Characterization and Chemical Synthesis of Cm39 (α-KTx 4.8) : a Scorpion Toxin That Inhibits Voltage-Gated K+ Channel KV1.2 and Small- and Intermediate-Conductance Ca2+-Activated K+ Channels KCa2.2 and KCa3.1 / Muhammad Umair Naseem, Georgina Gurrola-Briones, Margarita R. Romero-Imbachi, Jesus Borrego, Edson Carcamo-Noriega, José Beltrán-Vidal, Fernando Z. Zamudio, Kashmala Shakeel, Lourival Domingos Possani, Gyorgy Panyi
Dátum:	2023
ISSN:	2072-6651
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Cm39 scorpion toxin Centruroides margaritatus KV1.2 KCa2.2 KCa3.1 electrophysiology Ca2+-activated channel
Megjelenés:	Toxins. - 15 : 1 (2023), p. 1-21. -
További szerzők:	Gurrola-Briones, Georgina Romero-Imbachi, Margarita R. Borrego, Jesús Carcamo-Noriega, Edson Beltrán-Vidal, José Zamudio, Fernando Z. Shakeel, Kashmala Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	K143071 OTKA
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001-es BibID:	BIBFORM043018
035-os BibID:	PMID:22622363
Első szerző:	Varga Zoltán (biofizikus, szakfordító)
Cím:	Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells / Zoltan Varga, Georgina Gurrola-Briones, Ferenc Papp, Ricardo C. Rodríguez de la Vega, Gustavo Pedraza-Alva, Rajeev B. Tajhya, Rezso Gaspar, Luis Cardenas, Yvonne Rosenstein, Christine Beeton, Lourival D. Possani, Gyorgy Panyi
Dátum:	2012
Megjegyzések:	Blockade of Kv1.3 K(+) channels in T cells is a promising therapeutic approach for the treatment of autoimmune diseases such as multiple sclerosis and type 1 diabetes mellitus. Vm24 (alpha-KTx 23.1) is a novel 36-residue Kv1.3-specific peptide isolated from the venom of the scorpion Vaejovis mexicanus smithi. Vm24 inhibits Kv1.3 channels of human lymphocytes with high affinity (K(d) = 2.9 pM) and exhibits >1500-fold selectivity over other ion channels assayed. It inhibits the proliferation and Ca(2+) signaling of human T cells in vitro and reduces delayed-type hypersensitivity reactions in rats in vivo. Our results indicate that Vm24 has exceptional pharmacological properties that make it an excellent candidate for treatment of certain autoimmune diseases
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban article Autoimmune Diseases Biophysics cell biology Cells Human Hungary In Vitro Ion Channels Kv1.3 Potassium Channel lymphocyte Lymphocytes Multiple Sclerosis Potassium Potassium Channels Rats külföldön készült közlemény
Megjelenés:	Molecular Pharmacology. - 82 : 3 (2012), p. 372-382. -
További szerzők:	Gurrola-Briones, Georgina Papp Ferenc (1979-) (biofizikus) Rodríguez, Ricardo C. de la Vega Pedraza-Alva, Gustavo Tajhya, Rajeev B. Gáspár Rezső (1944-) (biofizikus) Cardenas, Luis Rosenstein, Yvonne Beeton, Christine Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	TÁMOP-4.2.2-08/1/2008-0019 TÁMOP TÁMOP-4.2.1/B-09/1/KONV-2010-007 TÁMOP TÁMOP-4.2.2-A-11/1/KONV-2012-0025 TÁMOP
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