@article{MTMT:34067941,
	title = {Synthesis and in vitro photodynamic activity of aza-BODIPY-based photosensitizers},
	url = {https://m2.mtmt.hu/api/publication/34067941},
	author = {Hlogyik, Tamás and Laczkó-Rigó, Réka and Bakos, Éva and Poór, Miklós and Kele, Zoltán and Laczka, Csilla and Mernyák, Erzsébet},
	doi = {10.1039/d3ob00699a},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {21},
	unique-id = {34067941},
	issn = {1477-0520},
	abstract = {Aza-BODIPY dyes have recently come to attention owing to their excellent chemical and photophysical properties. In particular, their absorption and emission maxima can efficiently be shifted to the red or even to the NIR spectral region. On this basis, aza-BODIPY derivatives are widely investigated as fluorescent probes or phototherapeutic agents. Here we report the synthesis of a set of novel aza-BODIPY derivatives as potential photosensitizers for use in photodynamic therapy. Triazolyl derivatives were obtained via Cu(I)-catalyzed azide-alkyne cycloaddition as the key step. In vitro photodynamic activities of the newly synthesized compounds were evaluated on the A431 human epidermoid carcinoma cell line. Structural differences influenced the light-induced toxicity of the test compounds markedly. Compared to the initial tetraphenyl aza-BODIPY derivative, the compound bearing two hydrophilic triethylene glycol side chains showed substantial, more than 250-fold, photodynamic activity with no dark toxicity. Our newly synthesized aza-BODIPY derivative, acting in the nanomolar range, might serve as a promising candidate for the design of more active and selective photosensitizers.},
	year = {2023},
	eissn = {1477-0539},
	pages = {6018-6027},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Mernyák, Erzsébet/0000-0003-4494-1817}
}

@article{MTMT:34043894,
	title = {Light-Fueled Primitive Replication and Selection in Biomimetic Chemical Systems},
	url = {https://m2.mtmt.hu/api/publication/34043894},
	author = {Bartus, Éva and Tököli, Attila and Mag, Beáta Zsófia and Bajcsi, Áron and Kecskeméti, Gábor and Wéber, Edit and Kele, Zoltán and Fenteany, Gabriel and Martinek, Tamás},
	doi = {10.1021/jacs.3c03597},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {145},
	unique-id = {34043894},
	issn = {0002-7863},
	abstract = {The concept of chemically evolvable replicators is centralto abiogenesis.Chemical evolvability requires three essential components: energy-harvestingmechanisms for nonequilibrium dissipation, kinetically asymmetricreplication and decomposition pathways, and structure-dependent selectivetemplating in the autocatalytic cycles. We observed a UVA light-fueledchemical system displaying sequence-dependent replication and replicatordecomposition. The system was constructed with primitive peptidicfoldamer components. The photocatalytic formation-recombinationcycle of thiyl radicals was coupled with the molecular recognitionsteps in the replication cycles. Thiyl radical-mediated chain reactionwas responsible for the replicator death mechanism. The competingand kinetically asymmetric replication and decomposition processesled to light intensity-dependent selection far from equilibrium. Here,we show that this system can dynamically adapt to energy influx andseeding. The results highlight that mimicking chemical evolution isfeasible with primitive building blocks and simple chemical reactions.},
	keywords = {PEPTIDES; DRIVEN},
	year = {2023},
	eissn = {1520-5126},
	pages = {13371-13383},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Tököli, Attila/0000-0001-8413-3182; Kecskeméti, Gábor/0000-0002-5584-6869; Wéber, Edit/0000-0002-5904-0619; Kele, Zoltán/0000-0002-4401-0302; Fenteany, Gabriel/0000-0001-7407-2195; Martinek, Tamás/0000-0003-3168-8066}
}

@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}
}

@CONFERENCE{MTMT:33748284,
	title = {Biocontrol ability of rationally designed peptide derivatives of a novel Solanum lycopersicum L. antifungal defensin},
	url = {https://m2.mtmt.hu/api/publication/33748284},
	author = {Hilda, Vass and Váradi, Györgyi and Kele, Zoltán and Gábor, Rákhely and Poór, Péter and Tóth, Gábor and Galgóczi, László Norbert and Tóth, Liliána},
	booktitle = {16th European Conference on Fungal Genetics: Programme & Abstracts},
	unique-id = {33748284},
	year = {2023},
	pages = {478-479},
	orcid-numbers = {Váradi, Györgyi/0000-0001-7907-8908; Kele, Zoltán/0000-0002-4401-0302; Poór, Péter/0000-0002-4539-6358; Tóth, Gábor/0000-0002-3604-4385; Galgóczi, László Norbert/0000-0002-6976-8910; Tóth, Liliána/0000-0003-1400-6174}
}

@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}
}

@{MTMT:33250254,
	title = {Intracellular protein targets of Neosartorya (Aspergillus) fischeri antifungal protein 2 in Candida albicans},
	url = {https://m2.mtmt.hu/api/publication/33250254},
	author = {Dán, Kinga and Kele, Zoltán and Váradi, Györgyi and Tóth, Liliána and Tóth, Gábor and Rákhely, Gábor and Galgóczi, László Norbert},
	booktitle = {FEMS Conference on Microbiology in association with Serbian Society of Microbiology},
	unique-id = {33250254},
	year = {2022},
	pages = {808-809},
	orcid-numbers = {Kele, Zoltán/0000-0002-4401-0302; Váradi, Györgyi/0000-0001-7907-8908; Tóth, Liliána/0000-0003-1400-6174; Tóth, Gábor/0000-0002-3604-4385; Galgóczi, László Norbert/0000-0002-6976-8910}
}

@article{MTMT:33071352,
	title = {Synthesis of the extracellular domain of GLP-1R by chemical and biotechnological approaches},
	url = {https://m2.mtmt.hu/api/publication/33071352},
	author = {Szolomájer, János and Stráner, Pál and Kele, Zoltán and Tóth, Gábor and Perczel, András},
	doi = {10.1039/D2RA02784D},
	journal-iso = {RSC ADV},
	journal = {RSC ADVANCES},
	volume = {12},
	unique-id = {33071352},
	issn = {2046-2069},
	abstract = {The extracellular domain of the glucagon-like peptide-1 receptor, GLP-1R, is responsible for the binding of GLP-1, and a handful of additional agonists (such as exenatide, lixisenatide, and liraglutide) used daily for treating type II diabetes mellitus. Lead discovery and optimization, however, require binding studies, which, in turn, necessitate the total synthesis of GLP-1R, comprising 108 residues. A protein domain of 10–15 kDa size could be obtained either by expression in E. coli or by ligating solid-phase peptide synthesis (SPPS)-made fragments. However, direct overexpression fails to give a properly folded protein, as GLP-1R forms an inclusion body, which fails to refold due to improper disulfide pairing. Several bacterial strains, constructs, and fusion partners were probed and it was found that only co-expression with MBP gave a 3D-fold allowing the native disulfide bond pattern formation. Some fusion partners can act as covalently linked or in situ chaperones for guiding the refolding of GLP-1R toward success. Therefore, the bottleneck to preparing GPCR extracellular domains is the correct pairing of the Cys residues. As a proof-of-concept model, nGLP1-R was made by SPPS to form the purified full-length polypeptide chain, subjected to self-guided or spontaneous Cys pairing. However, the formation of correct SS-pairs was lagging behind any protocol in use support, and the bottleneck of large-scale protein production relies on the risky step of proper refolding, which is sometimes possible only if a suitable fusion partner effectively helps and catalysis of the correct disulfide formation.},
	year = {2022},
	eissn = {2046-2069},
	pages = {24278-24287},
	orcid-numbers = {Stráner, Pál/0000-0003-2240-8501; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:32818711,
	title = {Synthesis of Heterocycles and Nucleosides Forming Higher—Order Structures},
	url = {https://m2.mtmt.hu/api/publication/32818711},
	author = {Váradi, Zoltán and Paragi, Gábor and Kupihár, Zoltán and Kele, Zoltán and Kovács, Lajos},
	doi = {10.3390/ecsoc-25-11705},
	journal-iso = {CHEM PROC},
	journal = {CHEMISTRY PROCEEDINGS},
	volume = {8},
	unique-id = {32818711},
	year = {2022},
	eissn = {2673-4583},
	orcid-numbers = {Paragi, Gábor/0000-0001-5408-1748; Kupihár, Zoltán/0000-0001-5499-7617; Kele, Zoltán/0000-0002-4401-0302; Kovács, Lajos/0000-0002-0331-3980}
}

@article{MTMT:32770194,
	title = {Diversity-Oriented Synthesis Catalyzed by Diethylaminosulfur-Trifluoride—Preparation of New Antitumor Ecdysteroid Derivatives},
	url = {https://m2.mtmt.hu/api/publication/32770194},
	author = {Vágvölgyi, Máté and Kocsis, Endre and Nové, Márta and Szemerédi, Nikoletta and Spengler, Gabriella and Kele, Zoltán and Berkecz, Róbert and Gáti, Tamás and Tóth, Gábor and Hunyadi, Attila},
	doi = {10.3390/ijms23073447},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {23},
	unique-id = {32770194},
	issn = {1661-6596},
	abstract = {Fluorine represents a privileged building block in pharmaceutical chemistry. Diethylaminosulfur-trifluoride (DAST) is a reagent commonly used for replacement of alcoholic hydroxyl groups with fluorine and is also known to catalyze water elimination and cyclic Beckmann-rearrangement type reactions. In this work we aimed to use DAST for diversity-oriented semisynthetic transformation of natural products bearing multiple hydroxyl groups to prepare new bioactive compounds. Four ecdysteroids, including a new constituent of Cyanotis arachnoidea, were selected as starting materials for DAST-catalyzed transformations. The newly prepared compounds represented combinations of various structural changes DAST was known to catalyze, and a unique cyclopropane ring closure that was found for the first time. Several compounds demonstrated in vitro antitumor properties. A new 17-N-acetylecdysteroid (13) exerted potent antiproliferative activity and no cytotoxicity on drug susceptible and multi-drug resistant mouse T-cell lymphoma cells. Further, compound 13 acted in significant synergism with doxorubicin without detectable direct ABCB1 inhibition. Our results demonstrate that DAST is a versatile tool for diversity-oriented synthesis to expand chemical space towards new bioactive compounds.},
	keywords = {NMR; FLUORINATION; structure elucidation; natural product; ecdysteroid; Anticancer},
	year = {2022},
	eissn = {1422-0067},
	orcid-numbers = {Vágvölgyi, Máté/0000-0002-2233-9422; Spengler, Gabriella/0000-0001-8085-0950; Kele, Zoltán/0000-0002-4401-0302; Berkecz, Róbert/0000-0002-9076-2177; Hunyadi, Attila/0000-0003-0074-3472}
}

@article{MTMT:32132785,
	title = {Formation of mono- and binuclear complexes of Nd3+ with d-gluconate ions in hyperalkaline solutions – Composition, equilibria and structure},
	url = {https://m2.mtmt.hu/api/publication/32132785},
	author = {Böszörményi, Éva and Kása, Zsolt and Varga, Gábor and Kele, Zoltán and Kutus, Bence and Peintler, Gábor and Pálinkó, István and Sipos, Pál Miklós},
	doi = {10.1016/j.molliq.2021.117047},
	journal-iso = {J MOL LIQ},
	journal = {JOURNAL OF MOLECULAR LIQUIDS},
	volume = {346},
	unique-id = {32132785},
	issn = {0167-7322},
	year = {2022},
	eissn = {1873-3166},
	orcid-numbers = {Kása, Zsolt/0000-0003-4352-7761; Varga, Gábor/0000-0002-7131-1629; Kele, Zoltán/0000-0002-4401-0302; Kutus, Bence/0000-0001-5023-0152; Peintler, Gábor/0000-0001-5171-5346; Pálinkó, István/0000-0002-8508-309X; Sipos, Pál Miklós/0000-0003-1407-0950}
}