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001-es BibID:	BIBFORM091922
035-os BibID:	(cikkazonosító)107692
Első szerző:	Krishnarjuna, Bankala
Cím:	A disulfide-stabilised helical hairpin fold in acrorhagin I : an emerging structural motif in peptide toxins / Bankala Krishnarjuna, Punnepalli Sunanda, Jessica Villegas-Moreno, Agota Csoti, Rodrigo A. V. Morales, Dorothy C. C. Wai, Gyorgy Panyi, Peter Prentis, Raymond S. Norton
Dátum:	2021
ISSN:	1047-8477
Megjegyzések:	Acrorhagin I (U-AITX-Aeq5a) is a disulfide-rich peptide identified in the aggressive organs (acrorhagi) of the sea anemone Actinia equina. Previous studies (Toxicon 2005, 46:768-74) found that the peptide is toxic in crabs, although the structural and functional properties of acrorhagin I have not been reported. In this work, an Escherichia coli (BL21 strain) expression system was established for the preparation of 13C,15N-labelled acrorhagin I, and the solution structure was determined using NMR spectroscopy. Structurally, acrorhagin I is similar to B-IV toxin from the marine worm Cerebratulus lacteus (PDB id 1VIB), with a well-defined helical hairpin structure stabilised by four intramolecular disulfide bonds. The recombinant peptide was tested in patch-clamp electrophysiology assays against voltage-gated potassium and sodium channels, and in bacterial and fungal growth inhibitory assays and haemolytic assays. Acrorhagin I was not active against any of the ion channels tested and showed no activity in functional assays, indicating that this peptide may possess a different biological function. Metal ion interaction studies using NMR spectroscopy showed that acrorhagin I bound zinc and nickel, suggesting that its function might be modulated by metal ions or that it may be involved in regulating metal ion levels and their transport. The similarity between the structure of acrorhagin I and that of B-IV toxin from a marine worm suggests that this fold may prove to be a recurring motif in disulfide-rich peptides from marine organisms.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk acrorhagin I NMR disulfides hairpin structure metal ion interaction sea anemone
Megjelenés:	Journal Of Structural Biology. - 213 : 2 (2021), p. 1-37. -
További szerzők:	Sunanda, Punnepalli Villegas-Moreno, Jessica Csóti Ágota (1989-) (biológus) Morales, Rodrigo A. V. Wai, Dorothy C. C. Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
Pályázati támogatás:	K119417 OTKA EFOP-3.6.1-16-2016-00022 EFOP GINOP-2.3.2-15-2016-00015 GINOP
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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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