@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:34136939,
	title = {Peptide and Peptidomimetic Assemblies in Dynamic Combinatorial Chemistry},
	url = {https://m2.mtmt.hu/api/publication/34136939},
	author = {Rodrigues, Ashmi and Rocard, Lou and Moumne, Roba},
	doi = {10.1002/syst.202300011},
	journal-iso = {CHEMSYSTEMSCHEM},
	journal = {CHEMSYSTEMSCHEM},
	unique-id = {34136939},
	year = {2023},
	eissn = {2570-4206}
}

@article{MTMT:34127153,
	title = {Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification},
	url = {https://m2.mtmt.hu/api/publication/34127153},
	author = {Yu, Z. and Kreitler, D.F. and Chiu, Y.T.T. and Xu, R. and Bruchs, A.T. and Bingman, C.A. and Gellman, S.H.},
	doi = {10.1002/anie.202308100},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	unique-id = {34127153},
	issn = {1433-7851},
	year = {2023},
	eissn = {1521-3773}
}

@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}
}

@article{MTMT:33333699,
	title = {Dynamic Amino Acid Side-Chains Grafting on Folded Peptide Backbone},
	url = {https://m2.mtmt.hu/api/publication/33333699},
	author = {Zagiel, Benjamin and Peker, Taleen and Marquant, Rodrigue and Cazals, Guillaume and Webb, Gabrielle and Miclet, Emeric and Bich, Claudia and Sachon, Emmanuelle and Moumne, Roba},
	doi = {10.1002/chem.202200454},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {28},
	unique-id = {33333699},
	issn = {0947-6539},
	abstract = {An efficient strategy for the synthesis of large libraries of conformationally defined peptides is reported, using dynamic combinatorial chemistry as a tool to graft amino acid side chains on a well-ordered 3D (3-dimension) peptide backbone. Combining rationally designed scaffolds with combinatorial side chains selection represents an alternative method to access peptide libraries for structures that are not genetically encodable. This method would allow a breakthrough for the discovery of protein mimetic for unconventional targets for which little is known.},
	keywords = {Peptide Library; Dynamic combinatorial chemistry; scaffold grafting},
	year = {2022},
	eissn = {1521-3765},
	orcid-numbers = {Bich, Claudia/0000-0002-8243-4018; Moumne, Roba/0000-0002-1528-9033}
}

@article{MTMT:31733221,
	title = {NMR Spectroscopy of supramolecular chemistry on protein surfaces},
	url = {https://m2.mtmt.hu/api/publication/31733221},
	author = {Bayer, Peter and Matena, Anja and Beuck, Christine},
	doi = {10.3762/bjoc.16.203},
	journal-iso = {BEILSTEIN J ORG CHEM},
	journal = {BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {16},
	unique-id = {31733221},
	issn = {1860-5397},
	abstract = {As one of the few analytical methods that offer atomic resolution, NMR spectroscopy is a valuable tool to study the interaction of proteins with their interaction partners, both biomolecules and synthetic ligands. In recent years, the focus in chemistry has kept expanding from targeting small binding pockets in proteins to recognizing patches on protein surfaces, mostly via supramolecular chemistry, with the goal to modulate protein-protein interactions. Here we present NMR methods that have been applied to characterize these molecular interactions and discuss the challenges of this endeavor.},
	keywords = {NMR; MOLECULAR RECOGNITION; supramolecular chemistry; protein ligand interaction; protein surfaces},
	year = {2020},
	eissn = {1860-5397},
	pages = {2505-2522}
}

@article{MTMT:31733219,
	title = {Construction of Protein Probe with a His-tag and an Electron-transfer Peptide for a Target Protein Sensing},
	url = {https://m2.mtmt.hu/api/publication/31733219},
	author = {Sugawara, Kazuharu and Ishizaki, Sora and Kikuchi, Soya and Kuramitz, Hideki and Kadoya, Toshihiko},
	doi = {10.1002/elan.202060338},
	journal-iso = {ELECTROANAL},
	journal = {ELECTROANALYSIS},
	unique-id = {31733219},
	issn = {1040-0397},
	abstract = {A protein probe with an electron-transfer peptide and a His-tag was designed to electrochemically sense a target protein. We selected tyrosine-rich (Y4C) and tryptophan-rich (W4C) peptides for use as electron-transfer agents. The peak for oxidation was based on the oxidations of the phenolic hydroxy groups in Y4C and on the indole rings in W4C. Asialofetuin (ASF) with galactose residues was the protein probe, and a galactose recognition protein, soybean agglutinin (SBA), was the target protein. A protein probe composed of an amino acid and carbohydrate residue was expected to be biocompatible. When voltammetric measurements were performed using a glassy carbon electrode, the oxidation peaks of H6Y4C and ASF-H6Y4C appeared at the same potential. The peak current of ASF-H6Y4C was 4-fold that of H6Y4C because of the stronger adsorption of ASF-H6Y4C onto the electrode. The electrode response of ASF-H6Y4C with SBA was half that of ASF-H6Y4C alone. By contrast, the peak current of ASF-Y4CH6 was higher than that of ASF-H6Y4C, which was the result of a greater degree of contact between the Y4C moieties and an electrode. On the other hand, the voltammetric behaviors of ASF with W4C and a His-tag were similar to those with Y4C and a His-tag. The sensitivity of SBA using ASF-Y4CH6 was at the 10(-13) M level. To confirm the function of the sensing system, measurements were performed in human serum with SBA and ASF-Y4CH6. When SBA was added, the serum had a concentration that ranged between 5.0x10(-13) and 4.0x10(-12) M, and the amount of SBA that could be recovered ranged from 97 to 101%. Consequently, this system could be applied to the detection of SBA in serum.},
	keywords = {tryptophan; tyrosine; Electron-transfer peptid; Asialofetuin; Soybean agglutinin},
	year = {2020},
	eissn = {1521-4109}
}

@article{MTMT:31422293,
	title = {Micro-flow synthesis of beta-amino acid derivatives via a rapid dual activation approach},
	url = {https://m2.mtmt.hu/api/publication/31422293},
	author = {Sugisawa, Naoto and Nakamura, Hiroyuki and Fuse, Shinichiro},
	doi = {10.1039/d0cc01403f},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {56},
	unique-id = {31422293},
	issn = {1359-7345},
	abstract = {Rapid dual activation (<= 3.3 s) of both beta-amino acid N-carboxy anhydride and alkyl chloroformate for the synthesis of a beta-amino acid-derived scaffold was demonstrated. The key to success was the use of rapid mixing enabled by using a micro-flow reactor. The one-flow synthesis of 22 beta-amino acid derivatives was achieved.},
	year = {2020},
	eissn = {1364-548X},
	pages = {4527-4530},
	orcid-numbers = {Nakamura, Hiroyuki/0000-0002-4511-2984; Fuse, Shinichiro/0000-0002-6836-4180}
}

@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}
}

@mastersthesis{MTMT:33539503,
	title = {Design of bio-inspired catalysts based on a gamma-peptide foldamer architecture},
	url = {https://m2.mtmt.hu/api/publication/33539503},
	author = {Aguesseau, Julie},
	publisher = {Université Montpellier},
	unique-id = {33539503},
	year = {2019}
}

@article{MTMT:30535263,
	title = {Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation},
	url = {https://m2.mtmt.hu/api/publication/30535263},
	author = {Nekkaa, Imane and Bogdán, Dóra and Gáti, Tamás and Béni, Szabolcs and Juhász, Tünde and Palkó, Márta and Paragi, Gábor and Tóth, Gábor and Fülöp, Ferenc and Mándity, István},
	doi = {10.1039/c8cc10147g},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	volume = {55},
	unique-id = {30535263},
	issn = {1359-7345},
	abstract = {Enantiodiscriminative helix formation was observed for beta-peptide H14 helices. This observation is caused by the synperiplanar orientation of H-O atoms which is more unfavorable than those for H-H interaction. The 1,2 H-O interaction leads to the destruction of the helical structure. The introduction of a double C-C bond in the backbone rules out helix formation.},
	keywords = {SELECTIVITY; DESIGN; SECONDARY STRUCTURE; STABILITY; OLIGOMERS; AMINO-ACID; FOLDAMER HELICES},
	year = {2019},
	eissn = {1364-548X},
	pages = {3061-3064},
	orcid-numbers = {Bogdán, Dóra/0000-0003-4455-8914; Béni, Szabolcs/0000-0001-7056-6825; Palkó, Márta/0000-0002-8265-7377; Paragi, Gábor/0000-0001-5408-1748; Tóth, Gábor/0000-0002-3604-4385; Fülöp, Ferenc/0000-0003-1066-5287; Mándity, István/0000-0003-2865-6143}
}

@article{MTMT:30378683,
	title = {12/10-Helix in Mixed beta-Peptides Alternating Bicyclic and Acyclic beta-Amino Acids: Probing the Relationship between Bicyclic Side Chain and Helix Stability},
	url = {https://m2.mtmt.hu/api/publication/30378683},
	author = {Simon, Matthieu and Milbeo, Pierre and Liu, Hongtao and Andre, Christophe and Wenger, Emmanuel and Martinez, Jean and Amblard, Muriel and Aubert, Emmanuel and Legrand, Baptiste and Calmes, Monique},
	doi = {10.1002/chem.201804404},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {24},
	unique-id = {30378683},
	issn = {0947-6539},
	abstract = {12/10-Helices constitute suitable templates that can be used to design original structures. Nevertheless, they often suffer from a weak stability in polar solvents because they exhibit a mixed hydrogen-bond network resulting in a small macrodipole. In this work, stable and functionalizable 12/10-helices were developed by alternating a highly constrained beta(2, 3, 3)-trisubstituted bicyclic amino acid (S)-1-aminobicyclo[2.2.2]octane-2-carboxylic acid ((S)-ABOC) and an acyclic substituted beta-homologated proteinogenic amino acid (l-beta(3)-hAA). Based on NMR spectroscopic analysis, it was shown that such mixed beta-peptides display well-defined right-handed 12/10-helices in polar, apolar, and chaotropic solvents; that are, CD3OH, CDCl3, and [D-6]DMSO, respectively. The stability of the hydrogen bonds forming the C-10 and C-12 pseudocycles as well as the benefit provided by the use of the constrained bicyclic ABOC versus typical acyclic beta-amino acids sequences when designing 12/10-helix were investigated using NH/ND NMR exchange experiments and DFT calculations in various solvents. These studies showed that the beta(3)-hAA/(S)-ABOC helix displayed a more stable hydrogen-bond network through specific stabilization of the C-10 pseudocycles involving the bridgehead NH of the ABOC bicyclic scaffold.},
	keywords = {helical structures; PROTEIN MODELS; BETA-PEPTIDE; foldamer; bicyclic beta-amino acids; helical stabilization},
	year = {2018},
	eissn = {1521-3765},
	pages = {18795-18800}
}

@article{MTMT:27106548,
	title = {An NMR Method To Pinpoint Supramolecular Ligand Binding to Basic Residues on Proteins},
	url = {https://m2.mtmt.hu/api/publication/27106548},
	author = {Hogeweg, Anna and Sowislok, Andrea and Schrader, Thomas and Beuck, Christine},
	doi = {10.1002/anie.201707950},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {56},
	unique-id = {27106548},
	issn = {1433-7851},
	year = {2017},
	eissn = {1521-3773},
	pages = {14758-14762}
}

@article{MTMT:26876392,
	title = {Dynamic Covalent Chemistry of Aldehyde Enamines: Bi-III- and Sc-III-Catalysis of Amine-Enamine Exchange},
	url = {https://m2.mtmt.hu/api/publication/26876392},
	author = {Zhang, Yang and Xie, Sheng and Yan, Mingdi and Ramstroem, Olof},
	doi = {10.1002/chem.201702363},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {23},
	unique-id = {26876392},
	issn = {0947-6539},
	year = {2017},
	eissn = {1521-3765},
	pages = {11908-11912}
}