Találati lista | Tudóstér

001-es BibID:	BIBFORM089163
035-os BibID:	(cikkazonosító)600983 (WOS)000589965500001 (Scopus)85096189197
Első szerző:	Gao, Ying
Cím:	Induction of New Lactam Derivatives From the Endophytic Fungus Aplosporella javeedii Through an OSMAC Approach / Ying Gao, Fabian Stuhldreier, Laura Schmitt, Sebastian Wesselborg, Zhiyong Guo, Kun Zou, Attila Mándi, Tibor Kurtán, Zhen Liu, Peter Proksch
Dátum:	2020
ISSN:	1664-302X
Megjegyzések:	Fermentation of the endophytic fungus Aplosporella javeedii on solid rice medium in presence of either 3.5% NaNO3 or 3.5% monosodium glutamate caused a significant change of the fungal metabolite pattern compared to fungal controls grown only on rice. Chemical investigation of the former fungal extracts yielded 11 new lactam derivatives, aplosporellins A-K (2-12), in addition to the known compound, pramanicin A (1). All of these compounds were not detected when the fungus was grown on rice medium without these activators thereby indicating the power of this OSMAC approach. The structures of the new compounds were elucidated by one- and two- dimensional NMR spectroscopy, DFT-NMR calculations and by mass spectrometry as well as by comparison with the literature whereas the absolute configuration of the lactam core was determined by TDDFT-ECD and OR calculations. Pramanicin A (1) showed strong cytotoxicity against human lymphoma (Ramos) and leukemia (Jurkat J16) cells with IC50 values of 4.7 and 4.4 mM, respectively. Mechanistic studies indicated that 1 activates caspase-3 and induces apoptotic cell death.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Aplosporella javeedii lactam derivatives OSMAC approach DFT-NMR TDDFT-ECD OR calculations apoptosis
Megjelenés:	Frontiers in Microbiology. - 11 (2020), p. 1-13. -
További szerzők:	Stuhldreier, Fabian Schmitt, Laura Wesselborg, Sebastian Guo, Zhi-Yong Zou, Kun Mándi Attila (1981-) (vegyész, német szakfordító) Kurtán Tibor (1973-) (vegyész, angol szakfordító) Liu, Zhen Proksch, Peter
Pályázati támogatás:	GINOP-2.3.2-15-2016-00008 GINOP NKFI K120181 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM072756
035-os BibID:	(cikkazonosító)393 (WOS)000426785800002 (Scopus)85043257197
Első szerző:	Tóth Liliána
Cím:	Anti-Candidal Activity and Functional Mapping of Recombinant and Synthetic Neosartorya fischeri Antifungal Protein 2 (NFAP2) / Tóth Liliána, Váradi Györgyi, Borics Attila, Batta Gyula, Kele Zoltán, Vendrinszky Ákos, Tóth Roberta, Ficze Hargita, Tóth Gábor K., Vágvölgyi Csaba, Marx Florentine, Galgóczy László
Dátum:	2018
ISSN:	1664-302X
Megjegyzések:	The increasing number of life-threatening Candida infections caused by antifungal drug-resistant strains urges the development of new therapeutic strategies. The small, cysteine-rich, and cationic Neosartorya fischeri antifungal protein 2 (NFAP2) effectively inhibits the growth of Candida spp. Limiting factors of its future application, are the low-yield production by the native producer, unavailable information about potential clinical application, and the unsolved relationship between the structure and function. In the present study we adopted a Penicillium chrysogenum-based expression system for bulk production of recombinant NFAP2. Furthermore, solid-phase peptide synthesis and native chemical ligation were applied to produce synthetic NFAP2. The average yield of recombinant and synthetic NFAP2 was 40- and 16-times higher than in the native producer, respectively. Both proteins were correctly processed, folded, and proved to be heat-stable. They showed the same minimal inhibitory concentrations as the native NFAP2 against clinically relevant Candida spp. Minimal inhibitory concentrations were higher in RPMI 1640 mimicking the human inner fluid than in a low ionic strength medium. The recombinant NFAP2 interacted synergistically with fluconazole, the first-line Candida therapeutic agent and significantly decreased its effective in vitro concentrations in RPMI 1640. Functional mapping with synthetic peptide fragments of NFAP2 revealed that not the evolutionary conserved antimicrobial ?-core motif, but the mid-N-terminal part of the protein influences the antifungal activity that does not depend on the primary structure of this region. Preliminary nucleic magnetic resonance measurements signed that the produced recombinant NFAP2 is suitable for further structural investigations.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Neosartorya fischeri antifungal protein 2 recombinant protein protein synthesis anti-candidal activity protein structure functional mapping
Megjelenés:	Frontiers in Microbiology. - 9 : 393 (2018), p. 1-12. -
További szerzők:	Váradi Györgyi Borics Attila Batta Gyula (1953-) (molekula-szerkezet kutató) Kele Zoltán Vendrinszky Ákos Tóth Roberta Ficze Hargita Tóth Gábor K. Vágvölgyi Csaba Marx, Florentine Galgóczy László (1950-)
Pályázati támogatás:	PD 120808, ANN 122833, ANN 110821 OTKA GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.2-15-2016-00014 GINOP GINOP-2.3.2-15-2016-00035 GINOP
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: