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1.

001-es BibID:BIBFORM091525
035-os BibID:(scopus)85100002242 (wos)000612002300001
Első szerző:Alvarado, Diana
Cím:A Novel Insecticidal Spider Peptide that Affects the Mammalian Voltage-Gated Ion Channel hKv1.5 / Diana Alvarado, Samuel Cardoso-Arenas, Ligia-Luz Corrales-García, Herlinda Clement, Iván Arenas, Pavel Andrei Montero-Dominguez, Timoteo Olamendi-Portugal, Fernando Zamudio, Agota Csoti, Jesús Borrego, Gyorgy Panyi, Ferenc Papp, Gerardo Corzo
Dátum:2021
ISSN:1663-9812
Megjegyzések:Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, even for mammal species. In this work, thirty animal venoms were screened against hKv1.5, a potential target for atrial fibrillation therapy. The whole venom of the spider Oculicosa supermirabilis, which is also insecticidal to house crickets, caused voltage-gated potassium ion channel modulation in hKv1.5. Therefore, a peptide from the spider O. supermirabilis venom, named Osu1, was identified through HPLC reverse-phase fractionation. Osu1 displayed similar biological properties as the whole venom; so, the primary sequence of Osu1 was elucidated by both of N-terminal degradation and endoproteolytic cleavage. Based on its primary structure, a gene that codifies for Osu1 was constructed de novo from protein to DNA by reverse translation. A recombinant Osu1 was expressed using a pQE30 vector inside the E. coli SHuffle expression system. recombinant Osu1 had voltage-gated potassium ion channel modulation of human hKv1.5, and it was also as insecticidal as the native toxin. Due to its novel primary structure, and hypothesized disulfide pairing motif, Osu1 may represent a new family of spider toxins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
atrial fibrillation
Kv1.5
Oculicosa supermirabilis
recombinant expression
spider venom
Megjelenés:Frontiers in Pharmacology. - 11 (2021), p. 1-13. -
További szerzők:Cardoso-Arenas, Samuel Corrales-García, Ligia-Luz Clement, Herlinda Arénas Iván Montero-Dominguez, Pavel Andrei Olamendi-Portugal, Timoteo Zamudio, Fernando Z. Csóti Ágota (1989-) (biológus) Borrego, Jesús Panyi György (1966-) (biofizikus) Papp Ferenc (1979-) (biofizikus) Corzo, Gerardo
Pályázati támogatás:K119417
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
GINOP-2.3.2-15-2016-00015
GINOP
University of Debrecen, Faculty of Medicine, Bridging Fund
Egyéb
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2.

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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3.

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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4.

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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5.

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:

6.

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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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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