@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:33597958, title = {Improved Metal-Free Approach for the Synthesis of Protected Thiol Containing Thymidine Nucleoside Phosphoramidite and Its Application for the Synthesis of Ligatable Oligonucleotide Conjugates}, url = {https://m2.mtmt.hu/api/publication/33597958}, author = {Kupihár, Zoltán and Ferenc, Györgyi and Petrovicz, Vencel László and Fáy, Viktória R. and Kovács, Lajos and Martinek, Tamás and Hegedüs, Zsófia}, doi = {10.3390/pharmaceutics15010248}, journal-iso = {PHARMACEUTICS}, journal = {PHARMACEUTICS}, volume = {15}, unique-id = {33597958}, issn = {1999-4923}, abstract = {Oligonucleotide conjugates are versatile scaffolds that can be applied in DNA-based screening platforms and ligand display or as therapeutics. Several different chemical approaches are available for functionalizing oligonucleotides, which are often carried out on the 5′ or 3′ end. Modifying oligonucleotides in the middle of the sequence opens the possibility to ligate the conjugates and create DNA strands bearing multiple different ligands. Our goal was to establish a complete workflow that can be applied for such purposes from monomer synthesis to templated ligation. To achieve this, a monomer is required with an orthogonal functional group that can be incorporated internally into the oligonucleotide sequence. This is followed by conjugation with different molecules and ligation with the help of a complementary template. Here, we show the synthesis and the application of a thiol-modified thymidine nucleoside phosphoramidite to prepare ligatable oligonucleotide conjugates. The conjugations were performed both in solution and on solid phase, resulting in conjugates that can be assembled into multivalent oligonucleotides decorated with tissue-targeting peptides using templated ligation.}, year = {2023}, eissn = {1999-4923}, orcid-numbers = {Ferenc, Györgyi/0000-0002-3456-319X; Kovács, Lajos/0000-0002-0331-3980; Martinek, Tamás/0000-0003-3168-8066; Hegedüs, Zsófia/0000-0002-5546-8167} } @article{MTMT:34047583, title = {Degradation-free intracellular delivery of nanomolar antibodies through reading the lipid raft sugar code with peptidic tags}, url = {https://m2.mtmt.hu/api/publication/34047583}, author = {Martinek, Tamás and Imre, Norbert and Hetényi, Anasztázia and Szabo, Eniko and Bodnar, Brigitta and Szkalisity, Abel and Grof, Ilona and Bocsik, Alexandra and Deli, Maria A. and Horvath, Peter and Czibula, Agnes and Monostori, Eva}, journal-iso = {J PEPT SCI}, journal = {JOURNAL OF PEPTIDE SCIENCE}, volume = {28}, unique-id = {34047583}, issn = {1075-2617}, keywords = {Biochemistry & Molecular Biology}, year = {2022}, eissn = {1099-1387}, orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Hetényi, Anasztázia/0000-0001-8080-6992} } @article{MTMT:33225790, title = {Tilted State Population of Antimicrobial Peptide PGLa Is Coupled to the Transmembrane Potential}, url = {https://m2.mtmt.hu/api/publication/33225790}, author = {Németh, Lukács and Martinek, Tamás and Jójárt, Balázs}, doi = {10.1021/acs.jcim.2c00667}, journal-iso = {J CHEM INF MODEL}, journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING}, volume = {62}, unique-id = {33225790}, issn = {1549-9596}, year = {2022}, eissn = {1549-960X}, pages = {4963-4969}, orcid-numbers = {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 = {Martinek, Tamás/0000-0003-3168-8066; Nyitray, László/0000-0003-4717-5994} } @article{MTMT:32743393, title = {Phosphine(III)‐Triggered One‐Pot Domino Sequences towards 5,6‐Dihydropyridine‐2‐(1 H )‐One and Pyridine‐2(1 H )‐One Scaffolds}, url = {https://m2.mtmt.hu/api/publication/32743393}, author = {Makra, Zsófia and Madácsi, Ramóna and Martinek, Tamás and Bényei, Attila Csaba and Puskás, László and Gyuris, Márió and Kanizsai, Iván}, doi = {10.1002/adsc.202101370}, journal-iso = {ADV SYNTH CATAL}, journal = {ADVANCED SYNTHESIS & CATALYSIS}, volume = {364}, unique-id = {32743393}, issn = {1615-4150}, year = {2022}, eissn = {1615-4169}, pages = {1134-1143}, orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066} } @article{MTMT:32733913, title = {α/β-Peptides as Nanomolar Triggers of Lipid Raft-Mediated Endocytosis through GM1 Ganglioside Recognition}, url = {https://m2.mtmt.hu/api/publication/32733913}, author = {Hetényi, Anasztázia and Szabó, Enikő and Imre, Norbert and Nath Bhaumik, Kaushik and Tököli, Attila and Füzesi, Tamás and Hollandi, Réka and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Deli, Mária Anna and Martinek, Tamás}, doi = {10.3390/pharmaceutics14030580}, journal-iso = {PHARMACEUTICS}, journal = {PHARMACEUTICS}, volume = {14}, unique-id = {32733913}, issn = {1999-4923}, abstract = {Cell delivery of therapeutic macromolecules and nanoparticles is a critical drug development challenge. Translocation through lipid raft-mediated endocytic mechanisms is being sought, as it can avoid rapid lysosomal degradation. Here, we present a set of short alpha/beta-peptide tags with high affinity to the lipid raft-associated ganglioside GM1. These sequences induce effective internalization of the attached immunoglobulin cargo. The structural requirements of the GM1-peptide interaction are presented, and the importance of the membrane components are shown. The results contribute to the development of a receptor-based cell delivery platform.}, year = {2022}, eissn = {1999-4923}, orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Tököli, Attila/0000-0001-8413-3182; Monostori, Éva/0000-0002-7442-3562; Deli, Mária Anna/0000-0001-6084-6524; Martinek, Tamás/0000-0003-3168-8066} } @article{MTMT:32493048, title = {Rationally designed foldameric adjuvants enhance antibiotic efficacy via promoting membrane hyperpolarization}, url = {https://m2.mtmt.hu/api/publication/32493048}, author = {Nath Bhaumik, Kaushik and Hetényi, Anasztázia and Olajos, Gábor and Martins, Ana and Spohn, Réka and Németh, Lukács and Jójárt, Balázs and Szili, Petra and Dunai, Anett and Jangir, Pramod Kumar and Daruka, Lejla and Földesi, Imre and Kata, Diána and Pál, Csaba and Martinek, Tamás}, doi = {10.1039/D1ME00118C}, journal-iso = {MOL SYST DES ENG}, journal = {MOLECULAR SYSTEMS DESIGN & ENGINEERING}, volume = {7}, unique-id = {32493048}, issn = {2058-9689}, abstract = {The negative membrane potential of bacterial cells influences crucial cellular processes. Inspired by the molecular scaffold of the antimicrobial peptide PGLa, we have developed antimicrobial foldamers with a computer-guided design strategy. The novel PGLa analogues induce sustained membrane hyperpolarization. When co-administered as an adjuvant, the resulting compounds - PGLb1 and PGLb2 - have substantially reduced the level of antibiotic resistance of multi-drug resistant Escherichia coli, Klebsiella pneumoniae and Shigella flexneri clinical isolates. The observed antibiotic potentiation was mediated by hyperpolarization of the bacterial membrane caused by the alteration of cellular ion transport. Specifically, PGLb1 and PGLb2 are selective ionophores that enhance the Goldman-Hodgkin-Katz potential across the bacterial membrane. These findings indicate that manipulating bacterial membrane electrophysiology could be a valuable tool to overcome antimicrobial resistance.}, year = {2022}, eissn = {2058-9689}, pages = {21-33}, orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Jangir, Pramod Kumar/0000-0001-8330-0655; Földesi, Imre/0000-0002-3329-8136; Kata, Diána/0000-0002-4432-9380; Martinek, Tamás/0000-0003-3168-8066} } @article{MTMT:32570862, title = {Fehérje méretű molekulák humán sejtekbe juttatása lipid-raft mediált endocitózissal}, url = {https://m2.mtmt.hu/api/publication/32570862}, author = {Hetényi, Anasztázia and Imre, Norbert and Szabó, Enikő and Bodnár, Brigitta and Szkalisity, Ábel and Gróf, Ilona and Bocsik, Alexandra and Deli, Mária Anna and Horváth, Péter and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás}, journal-iso = {BIOKÉMIA}, journal = {BIOKÉMIA: A MAGYAR BIOKÉMIAI EGYESÜLET FOLYÓIRATA}, volume = {45}, unique-id = {32570862}, issn = {0133-8455}, year = {2021}, eissn = {2060-8152}, pages = {67-83}, orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Deli, Mária Anna/0000-0001-6084-6524; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066} }