@article{MTMT:34510717,
	title = {Dynamic Structures of Bioactive Proteins as Determined by Nuclear Magnetic Resonance},
	url = {https://m2.mtmt.hu/api/publication/34510717},
	author = {Tőke, Orsolya and Batta, Gyula},
	doi = {10.3390/ijms25010295},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {25},
	unique-id = {34510717},
	issn = {1661-6596},
	abstract = {According to “Panta rhei”, a phrase by the ancient Greeks, you cannot enter the same river two times [...]},
	year = {2024},
	eissn = {1422-0067},
	orcid-numbers = {Tőke, Orsolya/0000-0002-1741-1573; Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:34076091,
	title = {E. Kövér Katalin: 1956–2023},
	url = {https://m2.mtmt.hu/api/publication/34076091},
	author = {Batta, Gyula},
	journal-iso = {MAGY KEM LAP},
	journal = {MAGYAR KÉMIKUSOK LAPJA},
	volume = {78},
	unique-id = {34076091},
	issn = {0025-0163},
	year = {2023},
	eissn = {1588-1199},
	pages = {191-191},
	orcid-numbers = {Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:34065963,
	title = {In memoriam Kövér Katalin (1956-2023)},
	url = {https://m2.mtmt.hu/api/publication/34065963},
	author = {Szilágyi, László and Batta, Gyula},
	doi = {10.24100/MKF.2023.01.04},
	journal-iso = {MAGY KÉM FOLY KÉM KÖZL},
	journal = {MAGYAR KÉMIAI FOLYÓIRAT - KÉMIAI KÖZLEMÉNYEK (1997-)},
	volume = {129},
	unique-id = {34065963},
	issn = {1418-9933},
	year = {2023},
	eissn = {1418-8600},
	pages = {4-6},
	orcid-numbers = {Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:34043893,
	title = {Hard nut to crack: Solving the disulfide linkage pattern of the Neosartorya (Aspergillus) fischeri antifungal protein 2},
	url = {https://m2.mtmt.hu/api/publication/34043893},
	author = {Váradi, Györgyi and Kele, Zoltán and Czajlik, András and Borics, Attila and Bende, Gábor and Papp, Csaba Gergő and Rákhely, Gábor and Tóth, Gábor and Batta, Gyula and Galgóczi, László Norbert},
	doi = {10.1002/pro.4692},
	journal-iso = {PROTEIN SCI},
	journal = {PROTEIN SCIENCE},
	volume = {32},
	unique-id = {34043893},
	issn = {0961-8368},
	abstract = {As a consequence of the fast resistance spreading, a limited number of drugs are available to treat fungal infections. Therefore, there is an urgent need to develop new antifungal treatment strategies. The features of a disulfide bond-stabilized antifungal protein, NFAP2 secreted by the mold Neosartorya (Aspergillus) fischeri render it to be a promising template for future protein-based antifungal drug design, which requires knowledge about the native disulfide linkage pattern as it is one of the prerequisites for biological activity. However, in the lack of tryptic and chymotryptic proteolytic sites in the ACNCPNNCK sequence, the determination of the disulfide linkage pattern of NFAP2 is not easy with traditional mass spectrometry-based methods. According to in silico predictions working with a preliminary nuclear magnetic resonance (NMR) solution structure, two disulfide isomers of NFAP2 (abbacc and abbcac) were possible. Both were chemically synthesized; and comparative reversed-phase high-performance liquid chromatography, electronic circular dichroism and NMR spectroscopy analyses, and antifungal susceptibility and efficacy tests indicated that the abbcac is the native pattern. This knowledge allowed rational modification of NAFP2 to improve the antifungal efficacy and spectrum through the modulation of the evolutionarily conserved gamma-core region, which is responsible for the activity of several antimicrobial peptides. Disruption of the steric structure of NFAP2 upon gamma-core modification led to the conclusions that this motif may affect the formation of the biologically active three-dimensional structure, and that the gamma-core modulation is not an efficient tool to improve the antifungal efficacy or to change the antifungal spectrum of NFAP2.},
	keywords = {DYNAMICS; PREDICTION; DRUG DESIGN; BONDS; protein structure; ANTIFUNGAL PROTEIN; disulfide linkage pattern},
	year = {2023},
	eissn = {1469-896X},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Kele, Zoltán/0000-0002-4401-0302; Papp, Csaba Gergő/0000-0003-4450-0667; Rákhely, Gábor/0000-0003-2557-3641; Tóth, Gábor/0000-0002-3604-4385; Batta, Gyula/0000-0002-0442-1828; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@article{MTMT:33676645,
	title = {Confirmation of the Disulfide Connectivity and Strategies for Chemical Synthesis of the Four-Disulfide-Bond-Stabilized Aspergillus giganteus Antifungal Protein, AFP},
	url = {https://m2.mtmt.hu/api/publication/33676645},
	author = {Váradi, Györgyi and Batta, Gyula and Galgóczi, László Norbert and Hajdu, Dorottya Zsuzsanna and Fizil, Ádám and Czajlik, András and Virágh, Máté and Kele, Zoltán and Meyer, Vera and Jung, Sascha and Marx, Florentine and Tóth, Gábor},
	doi = {10.1021/acs.jnatprod.2c00954},
	journal-iso = {J NAT PROD},
	journal = {JOURNAL OF NATURAL PRODUCTS},
	volume = {86},
	unique-id = {33676645},
	issn = {0163-3864},
	abstract = {Emerging fungal infections require new, more efficient antifungal agents and therapies. AFP, a protein from Aspergillus giganteus with four disulfide bonds, is a promising candidate because it selectively inhibits the growth of filamentous fungi. In this work, the reduced form of AFP was prepared using native chemical ligation. The native protein was synthesized via oxidative folding with uniform protection for cysteine thiols. AFP's biological activity depends heavily on the pattern of natural disulfide bonds. Enzymatic digestion and MS analysis provide proof for interlocking disulfide topology (abcdabcd) that was previously assumed. With this knowledge, a semi-orthogonal thiol protection method was designed. By following this strategy, out of a possible 105, only 6 disulfide isomers formed and 1 of them proved to be identical with the native protein. This approach allows the synthesis of analogs for examining structure-activity relationships and, thus, preparing AFP variants with higher antifungal activity.},
	year = {2023},
	eissn = {1520-6025},
	pages = {782-790},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Batta, Gyula/0000-0002-0442-1828; Galgóczi, László Norbert/0000-0002-6976-8910; Fizil, Ádám/0000-0002-4815-5744; Virágh, Máté/0000-0002-2278-1288; Kele, Zoltán/0000-0002-4401-0302; Meyer, Vera/0000-0002-2298-2258; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:33550734,
	title = {DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study},
	url = {https://m2.mtmt.hu/api/publication/33550734},
	author = {Czajlik, András and Batta, Ágnes and Kerner, Kinga and Fizil, Ádám and Hajdu, Dorottya Zsuzsanna and Hadháziné Raics, Mária and E Kövér, Katalin and Batta, Gyula},
	doi = {10.3390/ijms24021208},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33550734},
	issn = {1661-6596},
	abstract = {PAF and related antifungal proteins are promising antimicrobial agents. They have highly stable folds around room temperature due to the presence of 3–4 disulfide bonds. However, unfolded states persist and contribute to the thermal equilibrium in aqueous solution, and low-populated states might influence their biological impact. To explore such equilibria during dimethyl sulfoxide (DMSO)-induced chemical unfolding, we studied PAF and its inactive variant PAFD19S using nuclear magnetic resonance (NMR) and differential scanning calorimetry (DSC). According to the NMR monitoring at 310 K, the folded structures disappear above 80 v/v% DMSO concentration, while the unfolding is completely reversible. Evaluation of a few resolved peaks from viscosity-compensated 15N-1H HSQC spectra of PAF yielded ∆G = 23 ± 7 kJ/M as the average value for NMR unfolding enthalpy. The NMR-based structures of PAF and the mutant in 50 v/v% DMSO/H2O mixtures were more similar in the mixed solvents then they were in water. The 15N NMR relaxation dynamics in the same mixtures verified the rigid backbones of the NMR-visible fractions of the proteins; still, enhanced dynamics around the termini and some loops were observed. DSC monitoring of the Tm melting point showed parabolic dependence on the DMSO molar fraction and suggested that PAF is more stable than the inactive PAFD19S. The DSC experiments were irreversible due to the applied broad temperature range, but still suggestive of the endothermic unfolding of PAF.},
	keywords = {PAF; disulfide bond; Differential scanning calorimetry (DSC); ANTIFUNGAL PROTEIN; nuclear magnetic resonance (NMR); DMSO-induced unfolding},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Fizil, Ádám/0000-0002-4815-5744; Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:33119096,
	title = {Semisynthetic teicoplanin derivatives with dual antimicrobial activity against SARS-CoV-2 and multiresistant bacteria},
	url = {https://m2.mtmt.hu/api/publication/33119096},
	author = {Bakai-Bereczki, Ilona and Vimberg, Vladimir and Lőrincz, Eszter Boglárka and Papp, Henrietta and Nagy, Lajos and Kéki, Sándor and Batta, Gyula and Mitrović, Ana and Kos, Janko and Zsigmond, Áron and Hajdú, István and Lőrincz, Zsolt and Bajusz, Dávid and Petri, László and Hodek, Jan and Jakab, Ferenc and Keserű, György Miklós and Weber, Jan and Naesens, Lieve and Herczegh, Pál and Borbás, Anikó},
	doi = {10.1038/s41598-022-20182-y},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {33119096},
	issn = {2045-2322},
	abstract = {Patients infected with SARS-CoV-2 risk co-infection with Gram-positive bacteria, which severely affects their prognosis. Antimicrobial drugs with dual antiviral and antibacterial activity would be very useful in this setting. Although glycopeptide antibiotics are well-known as strong antibacterial drugs, some of them are also active against RNA viruses like SARS-CoV-2. It has been shown that the antiviral and antibacterial efficacy can be enhanced by synthetic modifications. We here report the synthesis and biological evaluation of seven derivatives of teicoplanin bearing hydrophobic or superbasic side chain. All but one teicoplanin derivatives were effective in inhibiting SARS-CoV-2 replication in VeroE6 cells. One lipophilic and three perfluoroalkyl conjugates showed activity against SARS-CoV-2 in human Calu-3 cells and against HCoV-229E, an endemic human coronavirus, in HEL cells. Pseudovirus entry and enzyme inhibition assays established that the teicoplanin derivatives efficiently prevent the cathepsin-mediated endosomal entry of SARS-CoV-2, with some compounds inhibiting also the TMPRSS2-mediated surface entry route. The teicoplanin derivatives showed good to excellent activity against Gram-positive bacteria resistant to all approved glycopeptide antibiotics, due to their ability to dually bind to the bacterial membrane and cell-wall. To conclude, we identified three perfluoralkyl and one monoguanidine analog of teicoplanin as dual inhibitors of Gram-positive bacteria and SARS-CoV-2.},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Bakai-Bereczki, Ilona/0000-0003-4601-7257; Papp, Henrietta/0000-0003-3887-5657; Batta, Gyula/0000-0002-0442-1828; Bajusz, Dávid/0000-0003-4277-9481; Weber, Jan/0000-0002-2799-7352; Borbás, Anikó/0000-0001-8462-4547}
}

@article{MTMT:32924494,
	title = {The Importance of Mg2+‐free State in Nucleotide Exchange of Oncogenic K‐Ras Mutants},
	url = {https://m2.mtmt.hu/api/publication/32924494},
	author = {Pálfy, Gyula and Karancsiné Menyhárd, Dóra and Ákontz-Kiss, Hanna and Vida, István and Batta, Gyula and Tőke, Orsolya and Perczel, András},
	doi = {10.1002/chem.202201449},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {28},
	unique-id = {32924494},
	issn = {0947-6539},
	abstract = {For efficient targeting of oncogenic K-Ras interaction sites, a mechanistic picture of the Ras-cycle is necessary. Herein, we used NMR relaxation techniques and molecular dynamics simulations to decipher the role of slow dynamics in wild-type and three oncogenic P-loop mutants of K-Ras. Our measurements reveal a dominant two-state conformational exchange on the ms timescale in both GDP- and GTP-bound KRas. The identified low-populated higher energy state in GDPloaded K-Ras has a conformation reminiscent of a nucleotidebound/Mg2+-free state characterized by shortened β2/β3-strands and a partially released switch-I region preparing K-Ras for the interaction with the incoming nucleotide exchange factor and subsequent reactivation. By providing insight into mutationspecific differences in K-Ras structural dynamics, our systematic analysis improves our understanding of prolonged K-Ras signaling and may aid the development of allosteric inhibitors targeting nucleotide exchange in K-Ras.},
	keywords = {NMR spectroscopy; K-RAS; molecular dynamics; Slow dynamics; Ras cycle},
	year = {2022},
	eissn = {1521-3765},
	orcid-numbers = {Pálfy, Gyula/0000-0003-1590-5331; Karancsiné Menyhárd, Dóra/0000-0002-0095-5531; Batta, Gyula/0000-0002-0442-1828; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32625251,
	title = {Resonance assignment of the Shank1 PDZ domain},
	url = {https://m2.mtmt.hu/api/publication/32625251},
	author = {Sánta, Anna and Czajlik, András and Batta, Gyula and Péterfia, Bálint and Gáspári, Zoltán},
	doi = {10.1007/s12104-022-10069-4},
	journal-iso = {BIOMOL NMR ASSIGM},
	journal = {BIOMOLECULAR NMR ASSIGNMENTS},
	volume = {16},
	unique-id = {32625251},
	issn = {1874-2718},
	abstract = {Shank proteins are among the most abundant and well-studied postsynaptic scaffold proteins. Their PDZ domain has unique characteristics as one of its loop regions flanking the ligand-binding site is uniquely long and has also been implicated in the formation of PDZ dimers. Here we report the initial characterization of the Shank1 PDZ domain by solution NMR spectroscopy. The assigned chemical shifts are largely consistent with the common features of PDZ domains in general and the available Shank PDZ crystal structures in particular. Our analysis suggests that under the conditions investigated, the domain is monomeric and the unique loop harbors a short helical segment, observed in only one of the known X-ray structures so far. Our work stresses the importance of solution-state investigations to fully decipher the functional relevance of the structural and dynamical features unique to Shank PDZ domains.},
	keywords = {PDZ DOMAIN; Shank1; Helical propensity; Monomeric},
	year = {2022},
	eissn = {1874-270X},
	pages = {121-127},
	orcid-numbers = {Batta, Gyula/0000-0002-0442-1828}
}

@article{MTMT:32584830,
	title = {The First Dimeric Derivatives of the Glycopeptide Antibiotic Teicoplanin},
	url = {https://m2.mtmt.hu/api/publication/32584830},
	author = {Bakai-Bereczki, Ilona and Szűcs, Zsolt and Batta, Gyula and Nagy, Tamás Milán and Ostorházi, Eszter and E Kövér, Katalin and Borbás, Anikó and Herczegh, Pál},
	doi = {10.3390/ph15010077},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {15},
	unique-id = {32584830},
	abstract = {Various dimeric derivatives of the glycopeptide antibiotic teicoplanin were prepared with the aim of increasing the activity of the parent compound against glycopeptide-resistant bacteria, primarily vancomycin-resistant enterococci. Starting from teicoplanin, four covalent dimers were prepared in two orientations, using an α,!-bis-isothiocyanate linker. Formation of a dimeric cobalt coordination complex of an N-terminal L-histidyl derivative of teicoplanin pseudoaglycone has been detected and its antibacterial activity evaluated. The Co(III)-induced dimerization of the histidyl derivative was demonstrated by DOSY experiments. Both the covalent and the complex dimeric derivatives showed high activity against VanA teicoplanin-resistant enterococci, but their activity against other tested bacterial strains did not exceed that of the monomeric compounds.},
	keywords = {synthesis; antibacterial activity; DIMER; teicoplanin; DOSY NMR; Co(III) complex; pseudoaglycone},
	year = {2022},
	eissn = {1424-8247},
	orcid-numbers = {Bakai-Bereczki, Ilona/0000-0003-4601-7257; Batta, Gyula/0000-0002-0442-1828; Nagy, Tamás Milán/0000-0003-4766-1992; Ostorházi, Eszter/0000-0002-9459-7316; Borbás, Anikó/0000-0001-8462-4547}
}