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001-es BibID:	BIBFORM127417
035-os BibID:	(Scopus)85217647241 (WoS)001418685000001
Első szerző:	Gai, Jiawei
Cím:	Small disulfide proteins with antifungal impact: NMR experimental structures as compared to models of alphafold versions / Jiawei Gai, Márk File, Réka Erdei, András Czajlik, Florentine Marx, László Galgóczy, Györgyi Váradi, Gyula Batta
Dátum:	2025
ISSN:	1661-6596 1422-0067
Megjegyzések:	In response to the growth of emerging resistance to conventional antifungal drugs, antifungal proteins (AFPs) of filamentous Ascomycetes origin have been discovered in recent years. Understanding the structure of AFPs is crucial for elucidating their antifungal mechanisms and developing new therapeutic agents. While nuclear magnetic resonance (NMR) has proven effective in determining the structures of small proteins, some AFP structures remain unresolved, necessitating the use of alternative prediction methods. Through bioinformatics analysis and heatmaps of amino acid sequence identity and similarity matrix, we categorized AFPs into three major classes and six subcategories, revealing structural and bioactivity differences. We employed AlphaFold (AF) to predict the 3D structures of six different AFPs, with predictions compared to NMR-derived structures. The results demonstrated a high degree of consistency between AF and NMR structures, with AF excelling in structural quality assessment and accurately capturing complex disulfide bond patterns. Both AF2 and AF3 models outperform the NMR model in overall structural quality and coherence, with AF3 showing the best performance. However, the limitations of AF should be considered, including its reduced accuracy in predicting multi-metal ion complexes, suboptimal performance in highly flexible or disordered regions, and its inability to account for multiple conformers, as it generates only a single dominant structure. Moreover, while AF3 accurately predicts all disulfide bond patterns, AF2 falls short in this regard. This study verifies the reliability of AF in the structural prediction of cysteine-rich AFPs while highlighting these constraints, offering important support for the rational design of new protein-based antifungal drugs.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk antifungal proteins AlphaFold NMR disulfide proteins mini-protein
Megjelenés:	International Journal of Molecular Sciences. - 26 : 3 (2025), p. 1-25. -
További szerzők:	File Márk Erdei Réka Czajlik András (1975-) (gyógyszerész) Marx, Florentine Galgóczy László (1950-) Váradi Györgyi Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:	NKFIH FK 134343 Egyéb NKFIH K 146131 Egyéb GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.3-15-2016-00004 GINOP
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001-es BibID:	BIBFORM090862
035-os BibID:	(WoS)000622919300001 (Scopus)85099773383
Első szerző:	Izsépi László
Cím:	Bacterial Cell Wall Analogue Peptides Control the Oligomeric States and Activity of the Glycopeptide Antibiotic Eremomycin : solution NMR and Antimicrobial Studies / László Izsépi, Réka Erdei, Anna N. Tevyashova, Natalia E. Grammatikova, Andrey E. Shchekotikhin, Pál Herczegh, Gyula Batta
Dátum:	2021
ISSN:	1424-8247
Megjegyzések:	For some time, glycopeptide antibiotics have been considered the last line of defense against Methicillin-resistant Staphylococcus aureus (MRSA). However, vancomycin resistance of Gram-positive bacteria is an increasingly emerging worldwide health problem. The mode of action of glycopeptide antibiotics is essentially the binding of peptidoglycan cell-wall fragments terminating in the D-Ala-D-Ala sequence to the carboxylate anion binding pocket of the antibiotic. Dimerization of these antibiotics in aqueous solution was shown to persist and even to enhance the antibacterial effect in a co-operative manner. Some works based on solid state (ss) Nuclear Magnetic Resonance (NMR) studies questioned the presence of dimers under the conditions of ssNMR while in a few cases, higher-order oligomers associated with contiguous back-to-back and face-to-face dimers were observed in the crystal phase. However, it is not proved if such oligomers persist in aqueous solutions. With the aid of 15N-labelled eremomycin using 15N relaxation and diffusion NMR methods, we observed tetramers and octamers when the N-Ac-D-Ala-D-Ala dipeptide was added. To the contrary, the N-Ac-D-Ala or (N-Ac)2-L-Lys-D-Ala-D-Ala tripeptide did not induce higher-order oligomers. These observations are interesting examples of tailored supramolecular self-organization. New antimicrobial tests have also been carried out with these self-assemblies against MRSA and VRE (resistant) strains.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk glycopeptide resistance eremomycin dimer oligomer N-Ac-D-Ala-D-Ala ligand 15N relaxation diffusion NMR
Megjelenés:	Pharmaceuticals. - 14 : 2 (2021), p. 1-14. -
További szerzők:	Erdei Réka Tevyashova, Anna N. Grammatikova, Natalia E. Shchekotikhin, Andrey E. Herczegh Pál (1947-) (vegyész, antibiotikumkémikus) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.3-15-2016-00004 GINOP NKFIH K119509 Egyéb
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001-es BibID:	BIBFORM094439
035-os BibID:	(cikkazonosító)379 (WoS)000643364900001 (Scopus)85105365400
Első szerző:	Moiseenko, Elena I.
Cím:	Aminoalkylamides of Eremomycin Exhibit an Improved Antibacterial Activity / Elena I. Moiseenko, Réka Erdei, Natalia E. Grammatikova, Elena P. Mirchink, Elena B. Isakova, Eleonora R. Pereverzeva, Gyula Batta, Andrey E. Shchekotikhin
Dátum:	2021
ISSN:	1424-8247
Megjegyzések:	After decades, the glycopeptide vancomycin is still the preferred antibiotic against resistant strains of Gram-positive bacteria. Although its clinical use is strictly regulated, the gradual spread of vancomycin-resistant bacteria, such as glycopeptide-resistant and glycopeptide-intermediate Staphylococcus aureus and vancomycin-resistant Enterococcus spp., is a serious health problem. Based on the literature data and previous studies, our main goal was to assess the antimicrobial potential and to study the structure-activity relationship of new eremomycin aminoalkylamides. We designed and synthesized a series of new eremomycin amides in which eremomycin is conjugated with a hydrophobic arylalkyl group via an alkylenediamine spacer, and tested their antibacterial activities on a panel of Gram-positive strains that were sensitive and resistant to a "gold-standard" vancomycin. Based on the data obtained, the structure-activity relationships were investigated, and a lead compound was selected for in-depth testing. Research carried out using an in vivo model of staphylococcus sepsis, acute toxicity studies, and the estimated therapeutic index also showed the advantage of the selected eremomycin amide derivative in particular, as well as the chosen direction in general.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk glycopeptide antibiotics vancomycin eremomycin semisynthetic antibiotics Gram-positive antibacterial activity
Megjelenés:	Pharmaceuticals. - 14 : 4 (2021), p. 1-19. -
További szerzők:	Erdei Réka Grammatikova, Natalia E. Mirchink, Elena P. Isakova, Elena B. Pereverzeva, Eleonora R. Batta Gyula (1953-) (molekula-szerkezet kutató) Shchekotikhin, Andrey E.
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001-es BibID:	BIBFORM076534
035-os BibID:	(WoS)000454616600030 (Scopus)85059218639
Első szerző:	Tevyashova, Anna N.
Cím:	Synthesis and evaluation of biological activity for dual-acting antibiotics on the basis of azithromycin and glycopeptides / Anna N. Tevyashova, Elena N. Bychkova, Alexander M. Korolev, Elena B. Isakova, Elena P. Mirchink, Ilya A. Osterman, Réka Erdei, Zsolt Szücs, Gyula Batta
Dátum:	2019
ISSN:	0960-894X
Megjegyzések:	One of the promising directions of the combined approach is the design of dual-acting antibiotics ? heterodimeric structures on the basis of antimicrobial agents of different classes. In this study a novel series of azithromycin-glycopeptide conjugates were designed and synthesized. The structures of the obtained compounds were confirmed using NMR spectroscopy and mass spectrometry data including MS/MS analysis. All novel hybrid antibiotics were found to be either as active as azithromycin and vancomycin against Gram-positive bacterial strains or have superior activity in comparison with their parent antibiotics. One compound, eremomycin-azithromycin conjugate 16, demonstrated moderate activity against Enterococcus faecium and Enterococcus faecalis strains resistant to vancomycin, and equal to vancomycin's activity for the treatment of mice with Staphylococcus aureus sepsis.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Macrolide antibiotics Azithromycin Glycopeptide antibiotics Vancomycin Eremomycin Dual action antibiotics Antibacterial activity Mechanism of action
Megjelenés:	Bioorganic & Medicinal Chemistry Letters. - 29 : 2 (2019), p. 276-280. -
További szerzők:	Bychkova, Elena N. Korolev, Alexander M. Isakova, Elena B. Mirchink, Elena P. Osterman, Ilya A. Erdei Réka Szűcs Zsolt (1991-) (gyógyszerész) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:	GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.3-15-2016-00004 GINOP
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