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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
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