@article{MTMT:34043118,
	title = {Proline cis/trans Isomerization in Intrinsically Disordered Proteins and Peptides},
	url = {https://m2.mtmt.hu/api/publication/34043118},
	author = {Sebák, Fanni and Szolomájer, János and Papp, Nándor and Tóth, Gábor and Bodor, Andrea},
	doi = {10.31083/j.fbl2806127},
	journal-iso = {FRONT BIOSCI-LANDMARK},
	journal = {FRONTIERS IN BIOSCIENCE-LANDMARK},
	volume = {28},
	unique-id = {34043118},
	issn = {2768-6701},
	year = {2023},
	eissn = {2768-6698},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Szolomájer, János/0000-0003-1458-6156; Tóth, Gábor/0000-0002-3604-4385; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:33611580,
	title = {Enhanced Antibacterial Activity of Substituted Derivatives of NCR169C Peptide},
	url = {https://m2.mtmt.hu/api/publication/33611580},
	author = {Howan, Dian Herlinda Octorina and Jenei, Sándor and Szolomájer, János and Endre, Gabriella and Kondorosi, Éva and Tóth, Gábor},
	doi = {10.3390/ijms24032694},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33611580},
	issn = {1661-6596},
	abstract = {Medicago truncatula in symbiosis with its rhizobial bacterium partner produces more than 700 nodule-specific cysteine-rich (NCR) peptides with diverse physicochemical properties. Most of the cationic NCR peptides have antimicrobial activity and the potential to tackle antimicrobial resistance with their novel modes of action. This work focuses on the antibacterial activity of the NCR169 peptide derivatives as we previously demonstrated that the C-terminal sequence of NCR169 (NCR169C17–38) has antifungal activity, affecting the viability, morphology, and biofilm formation of various Candida species. Here, we show that NCR169C17–38 and its various substituted derivatives are also able to kill ESKAPE pathogens such as Enterococcus faecalis, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Escherichia coli. The replacement of the two cysteines with serines enhanced the antimicrobial activity against most of the tested bacteria, indicating that the formation of a disulfide bridge is not required. As tryptophan can play role in the interaction with bacterial membranes and thus in antibacterial activity, we replaced the tryptophans in the NCR169C17–38C12,17/S sequence with various modified tryptophans, namely 5-methyl tryptophan, 5-fluoro tryptophan, 6-fluoro tryptophan, 7-aza tryptophan, and 5-methoxy tryptophan, in the synthesis of NCR169C17–38C12,17/S analogs. The results demonstrate that the presence of modified fluorotryptophans can significantly enhance the antimicrobial activity without notable hemolytic effect, and this finding could be beneficial for the further development of new AMPs from the members of the NCR peptide family.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Szolomájer, János/0000-0003-1458-6156; Endre, Gabriella/0000-0001-9493-7395; Kondorosi, Éva/0000-0002-4065-8515; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:33085154,
	title = {Preparation of 3- O -, 5- O - and N -palmitoyl derivatives of fumonisin B 1 toxin and their characterisation with NMR and LC-HRMS methods},
	url = {https://m2.mtmt.hu/api/publication/33085154},
	author = {Angeli, Cserne and Nagy, Tamás Milán and Horváth, Levente and Varga, Mónika and Szekeres, András and Tóth, Gábor and Janáky, Tamás and Szolomájer, János and Kovács, Melinda and E Kövér, Katalin and Bartók, Tibor},
	doi = {10.1080/19440049.2022.2116112},
	journal-iso = {FOOD ADDIT CONTAM A},
	journal = {FOOD ADDITIVES AND CONTAMINANTS PART A - CHEMISTRY ANALYSIS CONTROL EXPOSURE AND RISK ASSESSMENT},
	volume = {39},
	unique-id = {33085154},
	issn = {1944-0049},
	abstract = {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.},
	keywords = {Fusarium; MYCOTOXIN; Fumonisin B1; acylated fumonisin; O-acyl-FB1; N-acyl-FB1; hidden fumonisin},
	year = {2022},
	eissn = {1944-0057},
	pages = {1759-1771},
	orcid-numbers = {Szekeres, András/0000-0003-1651-4623; Tóth, Gábor/0000-0002-3604-4385; Janáky, Tamás/0000-0002-6466-8283; Szolomájer, János/0000-0003-1458-6156; Kovács, Melinda/0000-0001-5988-3934}
}

@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:32491001,
	title = {Novel Lysine-Rich Delivery Peptides of Plant Origin ERD and Human S100: The Effect of Carboxyfluorescein Conjugation, Influence of Aromatic and Proline Residues, Cellular Internalization, and Penetration Ability},
	url = {https://m2.mtmt.hu/api/publication/32491001},
	author = {Sebák, Fanni and Horváth, Lilla and Kovács, Dániel and Szolomájer, János and Tóth, Gábor and Babiczky, Ákos and Bősze, Szilvia and Bodor, Andrea},
	doi = {10.1021/acsomega.1c04637},
	journal-iso = {ACS OMEGA},
	journal = {ACS OMEGA},
	volume = {6},
	unique-id = {32491001},
	issn = {2470-1343},
	abstract = {The need for novel drug delivery peptides is an important issue of the modern pharmaceutical research. Here, we test K-rich peptides from plant dehydrin ERD14 (ERD-A, ERD-B, and ERD-C) and the C-terminal CPP-resembling region of S100A4 (S100) using the 5(6)-carboxyfluorescein (Cf) tag at the N-terminus. Via a combined pH-dependent NMR and fluorescence study, we analyze the effect of the Cf conjugation/modification on the structural behavior, separately investigating the (5)-Cf and (6)-Cf forms. Flow cytometry results show that all peptides internalize; however, there is a slight difference between the cellular internalization of (5)- and (6)-Cf-peptides. We indicate the possible importance of residues with an aromatic sidechain and proline. We prove that ERD-A localizes mostly in the cytosol, ERD-B and S100 have partial colocalization with lysosomal staining, and ERD-C mainly localizes within vesicle-like compartments, while the uptake mechanism mainly occurs through energy-dependent paths.},
	year = {2021},
	eissn = {2470-1343},
	pages = {34470-34484},
	orcid-numbers = {Sebák, Fanni/0000-0001-9252-9961; Szolomájer, János/0000-0003-1458-6156; Tóth, Gábor/0000-0002-3604-4385; Bodor, Andrea/0000-0002-7422-298X}
}

@article{MTMT:31953278,
	title = {Symbiotic NCR Peptide Fragments Affect the Viability, Morphology and Biofilm Formation of Candida Species},
	url = {https://m2.mtmt.hu/api/publication/31953278},
	author = {Szerencsés, Bettina and Gácser, Attila and Endre, Gabriella and Racskóné Domonkos, Ildikó and Tiricz, Hilda and Vágvölgyi, Csaba and Szolomájer, János and Howan, Dian Herlinda Octorina and Tóth, Gábor and Pfeiffer, Ilona and Kondorosi, Éva},
	doi = {10.3390/ijms22073666},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {31953278},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Gácser, Attila/0000-0003-2939-9580; Vágvölgyi, Csaba/0000-0003-0009-7773; Szolomájer, János/0000-0003-1458-6156; Tóth, Gábor/0000-0002-3604-4385; Pfeiffer, Ilona/0000-0003-0680-7596; Kondorosi, Éva/0000-0002-4065-8515}
}

@{MTMT:31642870,
	title = {Design and synthesis of selective ion channel blocker peptide toxin analogues},
	url = {https://m2.mtmt.hu/api/publication/31642870},
	author = {Tóth, Gábor and Bogár, Ferenc and Bozsó, Zsolt and Szolomájer, János and Kele, Zoltán and Csóti, Ágota and Szántó, Gábor Tibor and Panyi, György},
	booktitle = {Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project},
	unique-id = {31642870},
	year = {2020},
	pages = {75},
	orcid-numbers = {Panyi, György/0000-0001-6227-3301}
}

@{MTMT:31642862,
	title = {Synthesis of ryanodine receptor selective charybdotoxin analogues},
	url = {https://m2.mtmt.hu/api/publication/31642862},
	author = {Tóth, Gábor and Bozsó, Zsolt and Szolomájer, János and Kele, Zoltán and Zoltán, Pethő and János, Almássy and Zoltán, Varga},
	booktitle = {Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project},
	unique-id = {31642862},
	year = {2020},
	pages = {74}
}

@article{MTMT:31281264,
	title = {Potent Chimeric Antimicrobial Derivatives of the Medicago truncatula NCR247 Symbiotic Peptide},
	url = {https://m2.mtmt.hu/api/publication/31281264},
	author = {Jenei, Sándor and Tiricz, Hilda and Szolomájer, János and Tímár, Edit and Klement, Éva and Al Bouni, Mohamad Anas and Lima, Rui and Kata, Diána and Harmati, Mária and Buzás, Krisztina and Földesi, Imre and Tóth, Gábor and Endre, Gabriella and Kondorosi, Éva},
	doi = {10.3389/fmicb.2020.00270},
	journal-iso = {FRONT MICROBIOL},
	journal = {FRONTIERS IN MICROBIOLOGY},
	volume = {11},
	unique-id = {31281264},
	issn = {1664-302X},
	abstract = {In Rhizobium-legume symbiosis, the bacteria are converted into nitrogen-fixing bacteroids. In many legume species, differentiation of the endosymbiotic bacteria is irreversible, culminating in definitive loss of their cell division ability. This terminal differentiation is mediated by plant peptides produced in the symbiotic cells. In Medicago truncatula more than similar to 700 nodule-specific cysteine-rich (NCR) peptides are involved in this process. We have shown previously that NCR247 and NCR335 have strong antimicrobial activity on various pathogenic bacteria and identified interaction of NCR247 with many bacterial proteins, including FtsZ and several ribosomal proteins, which prevent bacterial cell division and protein synthesis. In this study we designed and synthetized various derivatives of NCR247, including shorter fragments and various chimeric derivatives. The antimicrobial activity of these peptides was tested on the ESKAPE bacteria; Enterococcus faecalis, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Escherichia coli as a member of Enterobacteriaceae and in addition Listeria monocytogenes and Salmonella enterica. The 12 amino acid long C-terminal half of NCR247, NCR247C partially retained the antimicrobial activity and preserved the multitarget interactions with partners of NCR247. Nevertheless NCR247C became ineffective on S. aureus, P. aeruginosa, and L. monocytogenes. The chimeric derivatives obtained by fusion of NCR247C with other peptide fragments and particularly with a truncated mastoparan sequence significantly increased bactericidal activity and altered the antimicrobial spectrum. The minimal bactericidal concentration of the most potent derivatives was 1.6 mu M, which is remarkably lower than that of most classical antibiotics. The killing activity of the NCR247-based chimeric peptides was practically instant. Importantly, these peptides had no hemolytic activity or cytotoxicity on human cells. The properties of these NCR derivatives make them promising antimicrobials for clinical use.},
	keywords = {DIFFERENTIATION; ANTIMICROBIAL PEPTIDES; CELL-CYCLE; plant symbiotic nodule-specific cysteine-rich peptides; NCR247; ESKAPE bacteria; modes of antimicrobial activity; killing kinetics; bacterial targets},
	year = {2020},
	eissn = {1664-302X},
	orcid-numbers = {Szolomájer, János/0000-0003-1458-6156; Kata, Diána/0000-0002-4432-9380; Harmati, Mária/0000-0002-4875-5723; Buzás, Krisztina/0000-0001-8933-2033; Földesi, Imre/0000-0002-3329-8136; Tóth, Gábor/0000-0002-3604-4385; Kondorosi, Éva/0000-0002-4065-8515}
}

@article{MTMT:31848285,
	title = {Amino acids: Chemistry, diversity and physical properties},
	url = {https://m2.mtmt.hu/api/publication/31848285},
	author = {Zarándi, Márta and Szolomájer, János},
	doi = {10.1039/9781788010627-00001},
	journal-iso = {AMINO ACIDS PEPT PROTEIN},
	journal = {AMINO ACIDS PEPTIDES AND PROTEINS},
	volume = {42},
	unique-id = {31848285},
	issn = {1361-5904},
	abstract = {The occurrence, chemistry, resolution, and analysis of amino acids published in the literature from 2013 finished with the year of 2016 are reviewed in this Chapter which is arranged in sections similar to previous Volumes in this Specialist Periodical report. Scientific Papers published during 2013-2016 have been sourced mainly from the Web of Science databases and Pubmed on the internet and from scanning a selection of major journals. © 2018 The Royal Society of Chemistry.},
	year = {2018},
	eissn = {1465-1912},
	pages = {1-84},
	orcid-numbers = {Zarándi, Márta/0000-0002-2136-2946; Szolomájer, János/0000-0003-1458-6156}
}