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001-es BibID:	BIBFORM114859
035-os BibID:	(cikkazonosító)140952 (scopus)85170288156
Első szerző:	Elnahriry, Khaled A.
Cím:	Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni / Elnahriry Khaled A., Wai Dorothy C. C., Ashwood Lauren M., Naseem Muhammad Umair, Szanto Tibor G., Guo Shaodong, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:	2024
ISSN:	1570-9639
Megjegyzések:	Sea anemone venoms are complex mixtures of biologically active compounds, including disulfide-rich peptides, some of which have found applications as research tools, and others as therapeutic leads. Our recent transcriptomic and proteomic studies of the Australian sea anemone Telmatactis stephensoni identified a transcript for a peptide designated Tst2. Tst2 is a 38-residue peptide showing sequence similarity to peptide toxins known to interact with a range of ion channels (NaV, TRPV1, KV and CaV). Recombinant Tst2 (rTst2, which contains an additional Gly at the N-terminus) was produced by periplasmic expression in Escherichia coli, enabling the production of both unlabelled and uniformly 13C,15N?labelled peptide for functional assays and structural studies. The LC-MS profile of the recombinant Tst2 showed a pure peak with molecular mass 6 Da less than that of the reduced form of the peptide, indicating the successful formation of three disulfide bonds from its six cysteine residues. The solution structure of rTst2 was determined using multidimensional NMR spectroscopy and revealed that rTst2 adopts an inhibitor cystine knot (ICK) structure. rTst2 was screened using various functional assays, including patch?clamp electrophysiological and cytotoxicity assays. rTst2 was inactive against voltagegated sodium channels (NaV) and the human voltage-gated proton (hHv1) channel. rTst2 also did not possess cytotoxic activity when assessed against Drosophila melanogaster flies. However, the recombinant peptide at 100 nM showed >50% inhibition of the transient receptor potential subfamily V member 1 (TRPV1) and slight (~10%) inhibition of transient receptor potential subfamily A member 1 (TRPA1). Tst2 is thus a novel ICK inhibitor of the TRPV1 channel.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Sea anemone Disulfide-rich peptides Recombinant expression NMR spectroscopy ICK scaffold TRPV1 channel
Megjelenés:	Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1872 : 1 (2024), p. 1-13. -
További szerzők:	Wai, Dorothy C. C. Ashwood, Lauren M. Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) Guo, Shaodong Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
Pályázati támogatás:	K143071 OTKA Stipendium Hungaricum Scholarship from the Tempus Public Foundation Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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