@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:33712712,
	title = {Structural Adaptation of the Single-Stranded DNA-Binding Protein C-Terminal to DNA Metabolizing Partners Guides Inhibitor Design},
	url = {https://m2.mtmt.hu/api/publication/33712712},
	author = {Tököli, Attila and Bodnár, Brigitta and Bogár, Ferenc and Paragi, Gábor and Hetényi, Anasztázia and Bartus, Éva and Wéber, Edit and Hegedüs, Zsófia and Szabó, Zoltán and Kecskeméti, Gábor and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.3390/pharmaceutics15041032},
	journal-iso = {PHARMACEUTICS},
	journal = {PHARMACEUTICS},
	volume = {15},
	unique-id = {33712712},
	issn = {1999-4923},
	abstract = {Single-stranded DNA-binding protein (SSB) is a bacterial interaction hub and an appealing target for antimicrobial therapy. Understanding the structural adaptation of the disordered SSB C-terminus (SSB-Ct) to DNA metabolizing enzymes (e.g., ExoI and RecO) is essential for designing high-affinity SSB mimetic inhibitors. Molecular dynamics simulations revealed the transient interactions of SSB-Ct with two hot spots on ExoI and RecO. The residual flexibility of the peptide–protein complexes allows adaptive molecular recognition. Scanning with non-canonical amino acids revealed that modifications at both termini of SSB-Ct could increase the affinity, supporting the two-hot-spot binding model. Combining unnatural amino acid substitutions on both segments of the peptide resulted in enthalpy-enhanced affinity, accompanied by enthalpy–entropy compensation, as determined by isothermal calorimetry. NMR data and molecular modeling confirmed the reduced flexibility of the improved affinity complexes. Our results highlight that the SSB-Ct mimetics bind to the DNA metabolizing targets through the hot spots, interacting with both of segments of the ligands.},
	year = {2023},
	eissn = {1999-4923},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bogár, Ferenc/0000-0002-0611-1452; Paragi, Gábor/0000-0001-5408-1748; Hetényi, Anasztázia/0000-0001-8080-6992; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Hegedüs, Zsófia/0000-0002-5546-8167; Szabó, Zoltán/0000-0001-8278-8038; Kecskeméti, Gábor/0000-0002-5584-6869; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:32777033,
	title = {Promiscuity mapping of the S100 protein family using a high-throughput holdup assay},
	url = {https://m2.mtmt.hu/api/publication/32777033},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	doi = {10.1038/s41598-022-09574-2},
	journal-iso = {SCI REP},
	journal = {SCIENTIFIC REPORTS},
	volume = {12},
	unique-id = {32777033},
	issn = {2045-2322},
	year = {2022},
	eissn = {2045-2322},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@misc{MTMT:31867968,
	title = {Binding Profile Mapping of the S100 Protein Family Using a High-throughput Local Surface Mimetic Holdup Assay},
	url = {https://m2.mtmt.hu/api/publication/31867968},
	author = {Simon, Márton and Bartus, Éva and Mag, Beáta Zsófia and Boros, Eszter and Roszjár, Lea and Gógl, Gergő and Travé, Gilles and Martinek, Tamás and Nyitray, László},
	unique-id = {31867968},
	abstract = {S100 proteins are small, typically homodimeric, vertebrate-specific EF-hand proteins that establish Ca2+-dependent protein-protein interactions in the intra- and extracellular environment and are overexpressed in various pathologies. There are about 20 distinct human S100 proteins with numerous potential partner proteins. Here, we used a quantitative holdup assay to measure affinity profiles of most members of the S100 protein family against a library of chemically synthetized foldamers. The profiles allowed us to quantitatively map the binding promiscuity of each member towards the foldamer library. Since the library was designed to systematically contain most binary natural amino acid side chain combinations, the data also provide insight into the promiscuity of each S100 protein towards all potential naturally-occurring S100 partners in the human proteome. Such information will be precious for future drug design of modulators of S100 pathological activities.},
	year = {2020},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994}
}

@article{MTMT:31598466,
	title = {Proteomimetic surface fragments distinguish targets by function},
	url = {https://m2.mtmt.hu/api/publication/31598466},
	author = {Tököli, Attila and Mag, Beáta Zsófia and Bartus, Éva and Wéber, Edit and Szakonyi, Gerda and Simon, Márton and Czibula, Ágnes and Monostori, Éva and Nyitray, László and Martinek, Tamás},
	doi = {10.1039/d0sc03525d},
	journal-iso = {CHEM SCI},
	journal = {CHEMICAL SCIENCE},
	volume = {11},
	unique-id = {31598466},
	issn = {2041-6520},
	year = {2020},
	eissn = {2041-6539},
	pages = {10390-10398},
	orcid-numbers = {Tököli, Attila/0000-0001-8413-3182; Bartus, Éva/0000-0001-9976-6978; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Nyitray, László/0000-0003-4717-5994; Martinek, Tamás/0000-0003-3168-8066}
}

@misc{MTMT:31624662,
	title = {Fénnyel hajtott disszipatív kovalens kémia foldamer ligandumok optimalizálására},
	url = {https://m2.mtmt.hu/api/publication/31624662},
	author = {Bartus, Éva and Mag, Beáta Zsófia and Kecskeméti, Gábor and Kele, Zoltán and Martinek, Tamás},
	unique-id = {31624662},
	year = {2019},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Kecskeméti, Gábor/0000-0002-5584-6869; Kele, Zoltán/0000-0002-4401-0302; Martinek, Tamás/0000-0003-3168-8066}
}

@mastersthesis{MTMT:31269723,
	title = {Bottom-up design of foldamers for protein surface recognition},
	url = {https://m2.mtmt.hu/api/publication/31269723},
	author = {Bartus, Éva},
	doi = {10.14232/phd.10208},
	publisher = {SZTE},
	unique-id = {31269723},
	year = {2019},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978}
}

@article{MTMT:30310687,
	title = {Structural optimization of foldamer-dendrimer conjugates as multivalent agents against the toxic effects of amyloid beta oligomers},
	url = {https://m2.mtmt.hu/api/publication/30310687},
	author = {Bartus, Éva and Olajos, Gábor and Schuster, Ildikó and Bozsó, Zsolt and Deli, Mária Anna and Veszelka, Szilvia and Walter, Fruzsina and Datki, Zsolt László and Szakonyi, Zsolt and Martinek, Tamás and Fülöp, Lívia},
	doi = {10.3390/molecules23102523},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {23},
	unique-id = {30310687},
	issn = {1420-3049},
	abstract = {Alzheimer's disease is one of the most common chronic neurodegenerative disorders. Despite several in vivo and clinical studies, the cause of the disease is poorly understood. Currently, amyloid β (Aβ) peptide and its tendency to assemble into soluble oligomers are known as a main pathogenic event leading to the interruption of synapses and brain degeneration. Targeting neurotoxic Aβ oligomers can help recognize the disease at an early stage or it can be a potential therapeutic approach. Unnatural β-peptidic foldamers are successfully used against many different protein targets due to their favorable structural and pharmacokinetic properties compared to small molecule or protein-like drug candidates. We have previously reported a tetravalent foldamer-dendrimer conjugate which can selectively bind Aβ oligomers. Taking advantage of multivalency and foldamers, we synthesized different multivalent foldamer-based conjugates to optimize the geometry of the ligand. Isothermal titration calorimetry (ITC) was used to measure binding affinity to Aβ, thereafter 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) based tissue viability assay and impedance-based viability assay on SH-SY5Y cells were applied to monitor Aβ toxicity and protective effects of the compounds. Important factors for high binding affinity were determined and a good correlation was found between influencing the valence and the capability of the conjugates for Aβ binding.},
	keywords = {MOLECULAR RECOGNITION; protein aggregation; foldamer; Multivalency; amyloid β},
	year = {2018},
	eissn = {1420-3049},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Olajos, Gábor/0000-0002-2479-4891; Schuster, Ildikó/0000-0001-9997-5729; Bozsó, Zsolt/0000-0002-5713-3096; Deli, Mária Anna/0000-0001-6084-6524; Walter, Fruzsina/0000-0001-8145-2823; Datki, Zsolt László/0000-0002-2537-4741; Szakonyi, Zsolt/0000-0003-2432-8409; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Lívia/0000-0002-8010-0129}
}

@article{MTMT:3213189,
	title = {De Novo Modular Development of a Foldameric Protein-Protein Interaction Inhibitor for Separate Hot Spots: A Dynamic Covalent Assembly Approach},
	url = {https://m2.mtmt.hu/api/publication/3213189},
	author = {Bartus, Éva and Hegedüs, Zsófia and Wéber, Edit and Csipak, Brigitta and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.1002/open.201700012},
	journal-iso = {CHEMISTRYOPEN},
	journal = {CHEMISTRYOPEN},
	volume = {6},
	unique-id = {3213189},
	issn = {2191-1363},
	keywords = {FOLDAMERS; MOLECULAR RECOGNITION; PEPTIDOMIMETICS; protein–protein interactions; dynamic covalent chemistry},
	year = {2017},
	eissn = {2191-1363},
	pages = {236-241},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:3193785,
	title = {Multivalent foldamer-based affinity assay for selective recognition of Aβ oligomers},
	url = {https://m2.mtmt.hu/api/publication/3193785},
	author = {Olajos, Gábor and Bartus, Éva and Schuster, Ildikó and Lautner, Gergely and Gyurcsányi, Ervin Róbert and Szögi, Titanilla and Fülöp, Lívia and Martinek, Tamás},
	doi = {10.1016/j.aca.2017.01.013},
	journal-iso = {ANAL CHIM ACTA},
	journal = {ANALYTICA CHIMICA ACTA},
	volume = {960},
	unique-id = {3193785},
	issn = {0003-2670},
	abstract = {Abstract Mimicking the molecular recognition functionality of antibodies is a great challenge. Foldamers are attractive candidates because of their relatively small size and designable interaction surface. This paper describes a sandwich type enzyme-linked immunoassay with a tetravalent β-peptide foldamer helix array as capture element and enzyme labeled tracer antibodies. The assay was found to be selective to β-amyloid oligomeric species with surface features transiently present in ongoing aggregation. In optimized conditions, with special emphasis on the foldamer immobilization, a detection limit of 5 pM was achieved with a linear range of 10–500 pM. These results suggest that protein mimetic foldamers can be useful tools in biosensors and affinity assays.},
	keywords = {FOLDAMERS; MOLECULAR RECOGNITION; Antibody mimetics; Bioaffinity assay; β-Amyloid oligomers},
	year = {2017},
	eissn = {1873-4324},
	pages = {131-137},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Bartus, Éva/0000-0001-9976-6978; Schuster, Ildikó/0000-0001-9997-5729; Gyurcsányi, Ervin Róbert/0000-0002-9929-7865; Szögi, Titanilla/0000-0002-9854-7340; Fülöp, Lívia/0000-0002-8010-0129; Martinek, Tamás/0000-0003-3168-8066}
}