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001-es BibID:	BIBFORM104671
035-os BibID:	(WOS)000849833500001 (Scopus)85138012200
Első szerző:	Angeli, Cserne
Cím:	Preparation of 3-O-, 5-O- and N-Palmitoyl Derivatives of Fumonisin B1 Toxin and their Characterisation with NMR and HPLC-HRMS Methods / Cserne Angeli, Tamás Milán Nagy, Levente Horváth, Mónika Varga, András Szekeres, Gábor K. Tóth, Tamás Janáky, János Szolomájer, Melinda Kovács, Katalin E. Kövér, Tibor Bartók
Dátum:	2022
ISSN:	1944-0049 1944-0057
Megjegyzések:	We have previously published six esterified O-acyl (EFB1) and three N-acyl fumonisin B-1 derivatives extracted from rice cultures inoculated with Fusarium verticillioides, amongst these the identification of N-palmitoyl-FB1 has been clearly established in a spiking experiment. At that time, it was assumed that as in the case of O-acyl-FB1 derivatives, linoleic-, oleic- or palmitic acid esterify through the OH group on the 3C or 5C atom of the carbon chain of the fumonisins. In our most recent experiments, we have synthetically acylated the FB1 toxin and subsequently purified 3-O-palmitoyl- and 5-O-palmitoyl-FB1 toxins in addition to the N-palmitoyl-FB1 toxin. They were identified and characterised using H-1 and C-13 NMR as well as LC-HRMS. Our aim was the identification of the previously detected O-acyl-FB1 derivatives over the course of a spiking experiment, which were obtained through the solid-phase fermentation of Fusarium verticillioides. By spiking the three synthesized and identified components one-by-one into the fungal culture extract and analysing these cultures using LC-MS, it was clearly demonstrated that the F. verticillioides strain produced both the 5-O-palmitoyl-FB1 and N-palmitoyl-FB1 toxins, but did not produce 3-O-palmitoyl-FB1. Thus, it is highly probable that the components thought to be 3-O-acyl-(linoleoyl-, oleoyl-, palmitoyl-) FB1 derivatives in our previous communication are presumably 10-O-acyl-FB1 derivatives. Since these acylated FB1 derivatives can occur naturally in e.g. maize, the use of these synthesized components as reference materials is of great importance in order to obtain accurate qualitative and quantitative data on the occurrence of acylated fumonisins in different matrices including maize based feed samples. The production of these substances has also made it possible to test their toxicity in cell culture and small animal experiments.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Fusarium mycotoxin fumonisin B1 acylated fumonisin O-acyl-FB1 N-acyl-FB1 hidden fumonisin
Megjelenés:	Food Additives and Contaminants Part A - Chemistry Analysis Control Exposure & Risk Assessment. - 39 : 10 (2022), p. 1759-1771. -
További szerzők:	Nagy Tamás Milán (1993-) (vegyész, nmr) Horváth Levente Varga Mónika Szekeres András Tóth Gábor K. Janáky Tamás Szolomájer János Kovács Melinda Kövér Katalin, E. (1956-2023) (vegyész) Bartók Tibor
Pályázati támogatás:	GINOP-2.3.2-15-2016-00046 GINOP EFOP3.6.3-VEKOP-16-2017-00005 Egyéb
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001-es BibID:	BIBFORM062511
Első szerző:	Fehér Krisztina (vegyész)
Cím:	Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds / Krisztina Fehér, István Timári, Kinga Rákosi, János Szolomájer, Tünde Z. Illyés, Ádám Bartók, Zoltán Varga, György Panyi, Gábor K. Tóth, Katalin E. Kövér
Dátum:	2016
ISSN:	2041-6520 2041-6539
Megjegyzések:	Anuroctoxin (AnTx), a 35-amino-acid scorpion toxin containing four disulfide bridges, is a high affinity blocker of the voltage-gated potassium channel Kv1.3, but also blocks Kv1.2. To improve potential therapeutic use of the toxin, we have designed a double substituted analog, [N17A/F32T]-AnTx, which showed comparable Kv1.3 affinity to the wild-type peptide, but also a 2500-fold increase in the selectivity for Kv1.3 over Kv1.2. In the present study we have achieved the chemical synthesis of a Sec-analog in which all cysteine (Cys) residues have been replaced by selenocysteine (Sec) forming four diselenide bonds. To the best of our knowledge this is the first time to replace, by chemical synthesis, all disulfide bonds with isosteric diselenides in a peptide/protein. Gratifyingly, the key pharmacological properties of the Sec-[N17A/F32T]-AnTx are retained since the peptide is functionally active. We also propose here a combined experimental and theoretical approach including NOE- and 77Se-based NMR supplemented by MD simulations for conformational and dynamic characterization of the Sec-[N17A/F32T]-AnTx. Using this combined approach allowed us to attain unequivocal assignment of all four diselenide bonds and supplemental MD simulations allowed characterization of the conformational dynamics around each disulfide/diselenide bridge.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban peptide toxin ion channels disulfide bridge
Megjelenés:	Chemical Science 7 (2016), p. 2666-2673. -
További szerzők:	Timári István (1989-) (vegyész) Rákosi Kinga Szolomájer János Illyés Tünde Zita (1970-) (kémia-fizika szakos tanár) Bartók Ádám (1984-) (biotechnológus) Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Tóth Gábor K. Kövér Katalin, E. (1956-2023) (vegyész)
Pályázati támogatás:	TAMOP-4.2.2/A-11/1/KONV-2012-0025 TÁMOP TAMOP-4.2.2/A-11/1/KONV-2012-0035 TÁMOP OTKA K 75904 OTKA OTKA NK 101337 OTKA OTKA K 105459 OTKA KTIA_NAP_13-2-2015?0009 Egyéb KTIA_13_NAP-A-III/8 Egyéb
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