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001-es BibID:BIBFORM004855
Első szerző:Bagdány Miklós
Cím:Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes / Bagdany, M., Batista, C. V. F., Valdez-Cruz, N. A., Somodi, S., Rodriguez de la Vega, R. C., Licea, A. F., Varga, Z., Gaspar, R., Possani, L. D., Panyi, G.
Dátum:2005
Megjegyzések:The physiological function of T lymphocytes can be modulated selectively by peptide toxins acting on Kv1.3 K(+) channels. Because Kv1.3-specific peptide toxins are considered to have a significant therapeutic potential in the treatment of autoimmune diseases, the discovery of new toxins is highly motivated. Through chromatographic procedures and electrophysiological assays, using patch-clamp methodology, the isolation of a novel peptide named anuroctoxin was accomplished using the venom of the Mexican scorpion Anuroctonus phaiodactylus. It has 35 amino acid residues with a molecular weight of 4082.8, tightly bound by four disulfide bridges whose complete covalent structure was determined. It has a pyroglutamic acid at the N-terminal region and an amidated C-terminal residue. Sequence comparison and phylogenetic clustering analysis classifies anuroctoxin into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx 6.12). Patch-clamp experiments show that anuroctoxin is a high-affinity blocker of Kv1.3 channels of human T lymphocytes with a K(d) of 0.73 nM, and it does not block the Ca(2+)-activated IKCa1 K(+) channels. These two channels play different but important roles in T-lymphocyte activation. Furthermore, the toxin practically does not inhibit Shaker IR, mKv1.1, and rKv2.1 channels, whereas the affinity of anuroctoxin for hKv1.2 is almost an order of magnitude smaller than for Kv1.3. The pharmacological profile and the selectivity of this new toxin for Kv1.3 over IKCa1 may provide an important tool for the modulation of the immune system, especially in cases in which selective inhibition of Kv1.3 is required.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
antagonists & inhibitors
Autoimmune Diseases
Biophysics
chemistry
drug effects
Human
Humans
Hungary
Immune System
Intermediate-Conductance Calcium-Activated Potassium Channels
Ion Channels
isolation & purification
Kv1.3 Potassium Channel
Lymphocytes
Models,Molecular
Molecular Weight
pharmacology
Phylogeny
Potassium
Potassium Channel Blockers
Potassium Channels
Potassium Channels,Calcium-Activated
Potassium Channels,Voltage-Gated
Research
Scorpion Venoms
Sequence Alignment
Support
T-Lymphocytes
Toxins
Toxins,Biological
Megjelenés:Molecular Pharmacology. - 67 : 4 (2005), p. 1034-1044. -
További szerzők:Batista, Cesar V. F. Valdez-Cruz, Norma A. Somodi Sándor (1977-) (belgyógyász) Rodriguez de la Vega, Ricardo C. Licea, Alexei F. Varga Zoltán (1969-) (biofizikus, szakfordító) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:elektronikus változat
DOI
elektronikus változat
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2.

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
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM010358
Első szerző:Papp Ferenc (biofizikus)
Cím:Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus / Papp, F., Batista, C. V. F., Varga, Z., Herceg, M., Roman-Gonzalez, S. A., Gaspar, R., Possani, L. D., Panyi, G.
Dátum:2009
ISSN:0041-0101 (Print)
Megjegyzések:Using high-performance liquid chromatography Tst26, a novel potassium channel blocker peptide, was purified from the venom of the Brazilian scorpion Tityus stigmurus. its primary structure was determined by means of automatic Edman degradation and mass spectrometry analysis. The peptide is composed of 37 amino acid residues and tightly folded through three disulfide bridges, similar to other K+ channel blocking peptides purified from scorpion venoms. It contains the "essential dyad" for K+ channel recognition comprised of a lysine at position 27 and a tyrosine at position 36. Electrophysiological assays revealed that Tst26 blocked hKv1.2 and hKv1.3 channels with high affinity (K-d = 1.9 nM and 10.7 nM, respectively) while it did not affect several other ion channels (mKv1.1, hKv1.4, hKv1.5, hERG, hIKCa1, hBK, hNav1.5) tested at 10 nM concentration. The voltage-dependent steady-state parameters of K+ channel gating were unaffected by the toxin in both channels, but due to the fast association and dissociation kinetics Tst26 slowed the rate of inactivation of Kv1.3 channels. Based on the primary structure, the systematic nomenclature proposed for this peptide is alpha-KTx 4.6.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Chromatography
Ion Channels
Kinetics
Lysine
Mass Spectrometry
Peptides
Potassium
Scorpion Venoms
Spectrometry
Tyrosine
Megjelenés:Toxicon. - 54 : 4 (2009), p. 379-389. -
További szerzők:Batista, Cesar V. F. Varga Zoltán (1969-) (biofizikus, szakfordító) Herceg Mónika (biofizikus) Roman-Gonzalez, Sergio A. Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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