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1.

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
Borító:

2.

001-es BibID:BIBFORM038449
Első szerző:Batista, Cesar V. F.
Cím:Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities / Cesar V. F. Batista, Froylan Gómez-Lagunas, Ricardo C. Rodriguez de la Vega, Péter Hajdu, György Panyi, Rezső Gáspár, Lourival D. Possani
Dátum:2002
ISSN:1570-9639
Megjegyzések:Two novel toxic peptides (Tc30 and Tc32) were isolated and characterized from the venom of the Brazilian scorpion Tityus cambridgei. The first have 37 and the second 35 amino acid residues, with molecular masses of 3,871.8 and 3,521.5, respectively. Both contain three disulfide bridges but share only 27% identity. They are relatively potent inhibitors of K(+)-currents in human T lymphocytes with K(d) values of 10 nM for Tc32 and 16 nM for Tc30, but they are less potent or quite poor blockers of Shaker B K(+)-channels, with respective K(d) values of 74 nM and 4.7 microM. Tc30 has a lysine in position 27 and a tyrosine at position 36 identical to those of charybdotoxin. These two positions conform the dyad considered essential for activity. On the contrary, Tc32 has a serine in the position equivalent to lysine 27 of charybdotoxin and does not contain any aromatic amino acid. Due to its unique primary sequence and to its distinctive preference for K(+)-channels of T lymphocytes, it was classified as the first example of a new subfamily of K(+)-channel-specific peptides (alpha-KT x 18.1). Tc30 is a member of the Tityus toxin II-9 subfamily and was given the number alpha-KT x 4.4.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1601 : 2 (2002), p. 123-131. -
További szerzők:Gómez-Lagunas, Froylan Rodriguez de la Vega, Ricardo C. Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
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DOI
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3.

001-es BibID:BIBFORM005176
Első szerző:Corzo, Gerardo
Cím:A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venomof the scorpion Centruroides suffusus suffusus / Corzo G., Papp F., Varga Z., Barraza O., Espino-Solis P. G., Rodríguez de la Vega R. C., Gaspar R., Panyi G., Possani L. D.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Kv1.3 Potassium Channel
Potassium
Potassium Channels
Megjelenés:Biochemical Pharmacology 76 : 9 (2008), p. 1142-1154. -
További szerzők:Papp Ferenc (1979-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Barraza, Omar Espino-Solis, Pavel G. Rodriguez de la Vega, Ricardo C. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:

4.

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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DOI
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5.

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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6.

001-es BibID:BIBFORM086320
035-os BibID:(cikkazonosító)113782 (WoS)000527342900009 (Scopus)85077711551
Első szerző:Luna-Ramirez, Karen
Cím:Structural basis of the potency and selectivity of Urotoxin, a potent Kv1 blocker from scorpion venom / Karen Luna-Ramirez, Agota Csoti, Jeffrey R. McArthur, Yanni K. Y. Chin, Raveendra Anangi, Rosby del Carmen Najera, Lourival D. Possani, Glenn F. King, Gyorgy Panyi, Haibo Yu, David J. Adams, Rocio K. Finol-Urdaneta
Dátum:2020
ISSN:0006-2952
Megjegyzések:Urotoxin (?-KTx 6), a peptide from venom of the Australian scorpion Urodacus yaschenkoi, is the most potent inhibitor of Kv1.2 described to date (IC = 160 pM). The native peptide also inhibits Kv1.1, Kv1.3 and KCa3.1 with nanomolar affinity but its low abundance in venom precluded further studies of its actions. Here we produced recombinant Urotoxin (rUro) and characterized the molecular determinants of Kv1 channel inhibition. The 3D structure of rUro determined using NMR spectroscopy revealed a canonical cysteine-stabilised ?/? (CS?/?) fold. Functional assessment of rUro using patch-clamp electrophysiology revealed the importance of C-terminal amidation for potency against Kv1.1?1.3 and Kv1.5. Neutralization of the putative pore-blocking K25 residue in rUro by mutation to Ala resulted in a major decrease in rUro potency against all Kv channels tested, without perturbing the toxin's structure. Reciprocal mutations in the pore of Uro-sensitive Kv1.2 and Uro-resistant Kv1.5 channels revealed a direct interaction between Urotoxin and the Kv channel pore. Our experimental work supports postulating a mechanism of action in which occlusion of the permeation pathway by the K25 residue in Urotoxin is the basis of its Kv1 inhibitory activity. Docking analysis was consistent with occlusion of the pore by K25 and the requirement of a small, non-charged amino acid in the Kv1 channel vestibule to facilitate toxin-channel interactions. Finally, computational studies revealed key interactions between the amidated C-terminus of Urotoxin and a conserved Asp residue in the turret of Kv1 channels, offering a potential rationale for potency differences between native and recombinant Urotoxin.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biochemical Pharmacology. - 174 (2020), p. 1-15. -
További szerzők:Csóti Ágota (1989-) (biológus) McArthur, Jeffrey R. Chin, Yanni K. Y. Anangi, Raveendra Najera, Rosby del Carmen Possani, Lourival Domingos King, Glenn F. Panyi György (1966-) (biofizikus) Yu, Haibo Adams, David J. Finol-Urdaneta, Rocio K.
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
NKFIH K119417
Egyéb
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DOI
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7.

001-es BibID:BIBFORM052923
Első szerző:Luna-Ramirez, Karen
Cím:Structure, Molecular Modeling, and Function of the Novel Potassium Channel Blocker Urotoxin Isolated from the Venom of the Australian Scorpion Urodacus yaschenkoi / Karen Luna-Ramirez, Adam Bartok, Rita Restano-Cassulini, Veronica Quintero-Hernández, Fredy I. V. Coronas, Janni Christensen, Christine E. Wright, Gyorgy Panyi, Lourival D. Possani
Dátum:2014
ISSN:1521-0111
Megjegyzések:This communication reports the structural and functional characterization of urotoxin, the first K(+) channel toxin isolated from the venom of the Australian scorpion Urodacus yaschenkoi. It is a basic peptide consisting of 37 amino acids with an amidated C-terminal residue. Urotoxin contains eight cysteines forming four disulfide bridges with sequence similarities resembling the ?-potassium channel toxin 6 (?-KTx-6) subfamily of peptides; it was assigned the systematic number of ?-KTx-6.21. Urotoxin is a potent blocker of human voltage-gated potassium channel (Kv)1.2 channels, with an IC50 of 160 pM, whereas its affinity for other channels tested was in the nanomolar range (hKv1.1, IC50 = 253 nM; hKv1.3, IC50 = 91 nM; and hKCa3.1, IC50 = 70 nM). The toxin had no effect on hKv1.4, hKv1.5, human ether-ℓa-go-go-related gene type 1 (hERG1), or human ether-ℓa-go-go-like (hELK2) channels. Multiple sequence alignments from the venom gland transcriptome showed the existence of four other new peptides similar to urotoxin. Computer modeling of urotoxin's three-dimensional structure suggests the presence of the ?/?-scaffold characteristic of other scorpion toxins, although very likely forming an uncommon disulfide pairing pattern. Using molecular dynamics, a model for the binding of this peptide to human Kv1.2 and hKv1.1 channels is presented, along with the binding of an in silico mutant urotoxin (Lys25Ala) to both channels. Urotoxin enriches our knowledge of K(+) channel toxins and, due to its high affinity for hKv1.2 channels, it may be a good candidate for the development of pharmacologic tools to study the physiologic functions of K(+) channels or related channelopathies and for restoring axonal conduction in demyelinated axons.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
scorpion toxin
potassium channel
Megjelenés:Molecular Pharmacology. - 86 : 1 (2014), p. 28-41. -
További szerzők:Bartók Ádám (1984-) (biotechnológus) Restano-Cassulini, Rita Quintero-Hernandez, Veronica Coronas, Fredy I. V. Christensen, Janni Wright, Christine E. Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
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8.

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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Intézményi repozitóriumban (DEA) tárolt változat
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9.

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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DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM069801
Első szerző:Olamendi-Portugal, Timoteo
Cím:Pi5 and Pi6, two undescribed peptides from the venom of the scorpion Pandinus imperator and their effects on K + -channels / Olamendi-Portugal T., Csoti A., Jimenez-Vargas J. M., Gomez-Lagunas F., Panyi G., Possani L. D.
Dátum:2017
ISSN:0041-0101
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Toxicon 133 (2017), p. 136-144. -
További szerzők:Csóti Ágota (1989-) (biológus) Jimenez-Vargas, J. M. Gómez-Lagunas, Froylan Panyi György (1966-) (biofizikus) Possani, Lourival Domingos
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11.

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
Internet cím:Szerző által megadott URL
DOI
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Borító:

12.

001-es BibID:BIBFORM004881
Első szerző:Olamendi-Portugal, Timoteo
Cím:Novel alpha-KTx peptides from the venom of the scorpion Centruroides elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells / Olamendi-Portugal, T., Somodi, S., Fernandez, J. A., Zamudio, F. Z., Becerril, B., Varga, Z., Panyi, G., Gaspar, R., Possani, L. D.
Dátum:2005
ISSN:0041-0101
Megjegyzések:From the venom of the Mexican scorpion Centruroides elegans Thorell five peptides were isolated to homogeneity by chromatographic procedures and their full amino acid sequence was determined by automatic Edman degradation. They all belong to the Noxiustoxin subfamily of scorpion toxins and were given the systematic names alpha-KTx 2.8 to 2.12, with trivial names Ce1 to Ce5, respectively. They have 39 amino acid residues, except for Ce3 which has only 38, but all of them have three disulfide bridges, and have molecular weights of 4255, 4267, 4249, 4295 and 4255 atomic mass units, respectively for Ce1 to Ce5. The C-terminal residues of Ce2, Ce4 and Ce5 were found to be amidated. The electrophysiological assay (whole-cell patch-clamp) showed that out of the five peptides, Ce1 (alpha-KTx 2.8), Ce2 (alpha-KTX2.9) and Ce4 (alpha-KTx 2.11) were effective blockers of Kv1.3 channels of human T lymphocytes, whereas these peptides did not inhibit the Ca2+-activated K+ channels (IKCa1) of the same cells. The equilibrium dissociation constants of these peptides for Kv1.3 were 0.70, 0.25 and 0.98nM for Ce1, Ce2 and Ce4, respectively. Furthermore, toxins Ce1, Ce2 and Ce4 practically did not inhibit the related voltage gated Shaker K+ channels, and rKv2.1 channels of the Shab family. The high affinity blockage of Kv1.3 channels by these peptides and their selectivity for Kv1.3 over IKCa1 may have significance in the development of novel tools for suppressing the function of those T cell subsets whose proliferation critically depends on the activity of Kv1.3 channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animals
antagonists & inhibitors
Bayes Theorem
Cell Line
Cells
chemistry
Chromatography,High Pressure Liquid
Comparative Study
Electrophysiology
Enzyme-Linked Immunosorbent Assay
genetics
Human
Humans
Intermediate-Conductance Calcium-Activated Potassium Channels
Kv1.3 Potassium Channel
Lymphocytes
Mass Spectrometry
metabolism
Mexico
Models,Genetic
Molecular Sequence Data
Molecular Weight
Organophosphorus Compounds
Peptides
Phylogeny
Potassium
Potassium Channels
Research
Scorpion Venoms
Scorpions
Sequence Analysis,Protein
Support
T-Lymphocytes
toxicity
Toxins
Megjelenés:Toxicon. - 46 : 4 (2005), p. 418-429. -
További szerzők:Somodi Sándor (1977-) (belgyógyász) Fernandez, Juan Antonio Zamudio, Fernando Z. Becerril, Baltazar Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
Internet cím:elektronikus változat
DOI
Borító:
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