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001-es BibID:	BIBFORM076189
Első szerző:	Krishnarjuna, Bankala
Cím:	Synthesis, folding, structure and activity of a predicted peptide from the sea anemone Oulactis sp. with an ShKT fold / Krishnarjuna Bankala, Villegas-Moreno Jessica, Mitchell Michela L., Csoti Agota, Peigneur Steve, Amero Carlos, Pennington Michael W., Tytgat Jan, Panyi Gyorgy, Norton Raymond S.
Dátum:	2018
ISSN:	0041-0101
Megjegyzések:	Sea anemone venom is rich in bioactive compounds, including peptides containing multiple disul?de bridges. In a transcriptomic study on Oulactis sp., we identi?ed the putative 36-residue peptide, OspTx2b, which is an isoform of the K channel blocker OspTx2a (Sunanda P et al. [2018] Identi?cation, chemical synthesis, structure and function of a new K V 1 channel blocking peptide from Oulactis sp. Peptide Science, in press). As OspTx2b contains a ShK/BgK-like cysteine framework, with high amino acid sequence similarity to BgK, we were interested to investigate its structure and function. The solution structure of OspTx2b was determined using nuclear magnetic resonance spectroscopy. OspTx2b does indeed possess a BgK-like sca?old, with the same disul?de bond connectivities. The orientation of the Lys-Tyr dyad in OspTx2b is more similar to that in ShK than in BgK. However, it failed to show against a range of voltage-gated potassium channels in Xenopus oocytes and human T lymphocytes. OspTx2b also showed no growth inhibitory activity against several strains of bacteria and fungi. Having a BgK-like fold with the Lys-Tyr dyad but no BgK-like activity highlights the importance of key amino acid residues in BgK that are missing in OspTx2b. The lack of activity against the KV channels assessed in this study emphasises that the ShK/BgK sca?old is capable of supporting functional activity beyond potassium channel blockade.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban OspTx2b Cysteine-rich peptide Sea anemone Structure NMR spectroscopy Potassium channel
Megjelenés:	Toxicon. - 150 (2018), p. 50-59. -
További szerzők:	Villegas-Moreno, Jessica Mitchell, Michela L. Csóti Ágota (1989-) (biológus) Peigneur, Steve Amero, Carlos Pennington, Michael W. Tytgat, Jan Panyi György (1966-) (biofizikus) Norton, Raymond S.
Pályázati támogatás:	Australian Research Council LP150100621 Egyéb Australian Government Research Training Program Scholarship and a Monash University?Museum Victoria Scholarship top-up Egyéb CELSA/17/047 - BOF/ISP Egyéb
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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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001-es BibID:	BIBFORM100131
Első szerző:	Reddiar, Sanjeevini Babu
Cím:	Lipopolysaccharide influences the plasma and brain pharmacokinetics of subcutaneously-administered HsTX1[R14A], a KV1.3-blocking peptide / Reddiar Sanjeevini Babu, Jin Liang, Wai Dorothy C. C., Csoti Agota, Panyi Gyorgy, Norton Raymond S., Nicolazzo Joseph A.
Dátum:	2021
ISSN:	0041-0101
Megjegyzések:	KV1.3 is a voltage-gated potassium channel that is upregulated in neuroinflammatory conditions, such as Alzheimer's disease and Parkinson's disease. HsTX1[R14A] is a potent and selective peptide blocker of KV1.3 with the potential to block microglial KV1.3, but its brain uptake is expected to be limited owing to the restrictive nature of the blood-brain barrier. To assess its peripheral and brain exposure, a LC-MS/MS assay was developed to quantify HsTX1[R14A] concentrations in mouse plasma and brain homogenate that was reliable and reproducible in the range of 6.7?66.7 nM (r2 = 0.9765) and 15?150 pmol/g (r2 = 0.9984), respectively. To assess if neuroinflammation affected HsTX1[R14A] disposition, C57BL/6 mice were administered HsTX1[R14A] subcutaneously (2 mg/kg) 24 h after an intraperitoneal dose of Escherichia coli lipopolysaccharide (LPS), which is commonly used to induce neuroinflammation; brain and plasma concentrations of HsTX1[R14A] were then quantified over 120 min. LPS treatment significantly retarded the decline in HsTX1[R14A] plasma concentrations, presumably as a result of reducing renal clearance, and led to substantial brain uptake of HsTX1[R14A], presumably through disruption of brain inter-endothelial tight junctions. This study suggests that HsTX1[R14A] may reach microglia in sufficient concentrations to block KV1.3 in neuroinflammatory conditions, and therefore has the potential to reduce neurodegenerative diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Toxicon. - 195 (2021), p. 29-36. -
További szerzők:	Jin, Liang Wai, Dorothy C. C. Csóti Ágota (1989-) (biológus) Panyi György (1966-) (biofizikus) Norton, Raymond S. Nicolazzo, Joseph A.
Pályázati támogatás:	K119417 OTKA EFOP-3.6.1-16-2016-00022 EFOP GINOP-2.3.2-15-2016-00015 GINOP
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