@mastersthesis{MTMT:34149712, title = {DESIGN STRATEGIES FOR PROTEIN-PROTEIN INTERACTION INHIBITORS USING NON-NATURAL AMINO ACIDS}, url = {https://m2.mtmt.hu/api/publication/34149712}, author = {Tököli, Attila}, unique-id = {34149712}, year = {2023}, orcid-numbers = {Tököli, Attila/0000-0001-8413-3182} } @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: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: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} }