TY - JOUR AU - Bartus, Éva AU - Tököli, Attila AU - Mag, Beáta Zsófia AU - Bajcsi, Áron AU - Kecskeméti, Gábor AU - Wéber, Edit AU - Kele, Zoltán AU - Fenteany, Gabriel AU - Martinek, Tamás TI - Light-Fueled Primitive Replication and Selection in Biomimetic Chemical Systems JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 145 PY - 2023 IS - 24 SP - 13371 EP - 13383 PG - 13 SN - 0002-7863 DO - 10.1021/jacs.3c03597 UR - https://m2.mtmt.hu/api/publication/34043894 ID - 34043894 AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Rodrigues, Ashmi AU - Rocard, Lou AU - Moumne, Roba TI - Peptide and Peptidomimetic Assemblies in Dynamic Combinatorial Chemistry JF - CHEMSYSTEMSCHEM J2 - CHEMSYSTEMSCHEM PY - 2023 SN - 2570-4206 DO - 10.1002/syst.202300011 UR - https://m2.mtmt.hu/api/publication/34136939 ID - 34136939 LA - English DB - MTMT ER - TY - JOUR AU - Yu, Z. AU - Kreitler, D.F. AU - Chiu, Y.T.T. AU - Xu, R. AU - Bruchs, A.T. AU - Bingman, C.A. AU - Gellman, S.H. TI - Harnessing Aromatic-Histidine Interactions through Synergistic Backbone Extension and Side Chain Modification JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT PY - 2023 SN - 1433-7851 DO - 10.1002/anie.202308100 UR - https://m2.mtmt.hu/api/publication/34127153 ID - 34127153 N1 - Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, United States National Synchrotron Light Source II, Brookhaven National Laboratory, Upton, NY 11973, United States Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, United States Export Date: 5 September 2023 CODEN: ACIEF Correspondence Address: Gellman, S.H.; Department of Chemistry, United States; email: gellman@chem.wisc.edu LA - English DB - MTMT ER - TY - JOUR AU - Simon, Márton AU - Bartus, Éva AU - Mag, Beáta Zsófia AU - Boros, Eszter AU - Roszjár, Lea AU - Gógl, Gergő AU - Travé, Gilles AU - Martinek, Tamás AU - Nyitray, László TI - Promiscuity mapping of the S100 protein family using a high-throughput holdup assay JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 12 PY - 2022 IS - 1 PG - 11 SN - 2045-2322 DO - 10.1038/s41598-022-09574-2 UR - https://m2.mtmt.hu/api/publication/32777033 ID - 32777033 N1 - These authors contributed equally: Márton A. Simon and Éva Bartus LA - English DB - MTMT ER - TY - JOUR AU - Zagiel, Benjamin AU - Peker, Taleen AU - Marquant, Rodrigue AU - Cazals, Guillaume AU - Webb, Gabrielle AU - Miclet, Emeric AU - Bich, Claudia AU - Sachon, Emmanuelle AU - Moumne, Roba TI - Dynamic Amino Acid Side-Chains Grafting on Folded Peptide Backbone JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 28 PY - 2022 IS - 36 PG - 8 SN - 0947-6539 DO - 10.1002/chem.202200454 UR - https://m2.mtmt.hu/api/publication/33333699 ID - 33333699 N1 - Sorbonne Université, École normale supérieure, PSL University, CNRS, Laboratoire des biomolécules, LBM, Paris, 75005, France UMR 5247-CNRS-UM-ENSCM, Institut des Biomolécules Max Mousseron (IBMM), Université de Montpellier, Montpellier, 34293, France MS3 U platform, UFR 926, UFR 927, Sorbonne Université, 4 place Jussieu, Paris, 75005, France Export Date: 8 September 2023 CODEN: CEUJE Correspondence Address: Moumné, R.; Sorbonne Université, France; email: roba.moumne@sorbonne-universite.fr AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Bayer, Peter AU - Matena, Anja AU - Beuck, Christine TI - NMR Spectroscopy of supramolecular chemistry on protein surfaces JF - BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY J2 - BEILSTEIN J ORG CHEM VL - 16 PY - 2020 SP - 2505 EP - 2522 PG - 18 SN - 1860-5397 DO - 10.3762/bjoc.16.203 UR - https://m2.mtmt.hu/api/publication/31733221 ID - 31733221 N1 - Cited By :3 Export Date: 8 September 2023 CODEN: BJOCB Correspondence Address: Beuck, C.; Structural and Medicinal Biochemistry, Universitätsstr. 1-5, Germany; email: christine.beuck@uni-due.de AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Sugawara, Kazuharu AU - Ishizaki, Sora AU - Kikuchi, Soya AU - Kuramitz, Hideki AU - Kadoya, Toshihiko TI - Construction of Protein Probe with a His-tag and an Electron-transfer Peptide for a Target Protein Sensing JF - ELECTROANALYSIS J2 - ELECTROANAL PY - 2020 PG - 13 SN - 1040-0397 DO - 10.1002/elan.202060338 UR - https://m2.mtmt.hu/api/publication/31733219 ID - 31733219 N1 - Maebashi Institute of Technology, Gunma, 371-0816, Japan Department of Environmental Biology and Chemistry, Graduate School of Science and Engineering for Research, University of Toyama, Toyama, 930-8555, Japan Cited By :2 Export Date: 8 September 2023 CODEN: ELANE Correspondence Address: Sugawara, K.; Maebashi Institute of TechnologyJapan; email: kzsuga@maebashi-it.ac.jp AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Sugisawa, Naoto AU - Nakamura, Hiroyuki AU - Fuse, Shinichiro TI - Micro-flow synthesis of beta-amino acid derivatives via a rapid dual activation approach JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 56 PY - 2020 IS - 33 SP - 4527 EP - 4530 PG - 4 SN - 1359-7345 DO - 10.1039/d0cc01403f UR - https://m2.mtmt.hu/api/publication/31422293 ID - 31422293 N1 - Cited By :11 Export Date: 6 September 2023 CODEN: CHCOF Correspondence Address: Fuse, S.; Department of Basic Medicinal Sciences, Japan; email: fuse@ps.nagoya-u.ac.jp AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Tököli, Attila AU - Mag, Beáta Zsófia AU - Bartus, Éva AU - Wéber, Edit AU - Szakonyi, Gerda AU - Simon, Márton AU - Czibula, Ágnes AU - Monostori, Éva AU - Nyitray, László AU - Martinek, Tamás TI - Proteomimetic surface fragments distinguish targets by function JF - CHEMICAL SCIENCE J2 - CHEM SCI VL - 11 PY - 2020 IS - 38 SP - 10390 EP - 10398 PG - 9 SN - 2041-6520 DO - 10.1039/d0sc03525d UR - https://m2.mtmt.hu/api/publication/31598466 ID - 31598466 N1 - Department of Medical Chemistry, University of Szeged, Dóm tér 8, Szeged, H6720, Hungary MTA-SZTE Biomimetic Systems Research Group, University of Szeged, Dóm tér 8, Szeged, H6720, Hungary Institute of Pharmaceutical Analysis, University of Szeged, Somogyi u. 4., Szeged, H6720, Hungary Department of Biochemistry, Eötvös Loránd University, Pázmány Péter sétány 1/C, Budapest, H1077, Hungary Lymphocyte Signal Transduction Laboratory, Institute of Genetics, Biological Research Centre, Temesvári krt. 62, H6726 Szeged, Hungary Cited By :3 Export Date: 12 March 2024 CODEN: CSHCC Correspondence Address: Nyitray, L.; Department of Biochemistry, Pázmány Péter sétány 1/C, Hungary; email: nyitray@elte.hu LA - English DB - MTMT ER - TY - THES AU - Aguesseau, Julie TI - Design of bio-inspired catalysts based on a gamma-peptide foldamer architecture PB - Université Montpellier PY - 2019 UR - https://m2.mtmt.hu/api/publication/33539503 ID - 33539503 LA - English DB - MTMT ER - TY - JOUR AU - Nekkaa, Imane AU - Bogdán, Dóra AU - Gáti, Tamás AU - Béni, Szabolcs AU - Juhász, Tünde AU - Palkó, Márta AU - Paragi, Gábor AU - Tóth, Gábor AU - Fülöp, Ferenc AU - Mándity, István TI - Flow-chemistry enabled efficient synthesis of β-peptides: backbone topology vs. helix formation JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN VL - 55 PY - 2019 IS - 21 SP - 3061 EP - 3064 PG - 4 SN - 1359-7345 DO - 10.1039/c8cc10147g UR - https://m2.mtmt.hu/api/publication/30535263 ID - 30535263 N1 - Funding Agency and Grant Number: Hungarian Research Foundation (OTKA) [K 115731]; Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences; Bolyai + New National Excellence Program of the Ministry of Human Capacities [UNKP-18-4-SE-121]; [GINOP-2.3.2-15-2016-00014]; [GINOP-2.3.2-15-2016-00034] Funding text: We are grateful to the Hungarian Research Foundation (OTKA No. K 115731). The financial support of the GINOP-2.3.2-15-2016-00014 and GINOP-2.3.2-15-2016-00034 projects are acknowledged. This work was partially supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and by the Bolyai + New National Excellence Program (grant number: UNKP-18-4-SE-121) of the Ministry of Human Capacities (S. Beni). Funding Agency and Grant Number: Hungarian Research Foundation (OTKA)Orszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [K 115731]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; Bolyai + New National Excellence Program of the Ministry of Human Capacities [UNKP-18-4-SE-121]; [GINOP-2.3.2-15-2016-00014]; [GINOP-2.3.2-15-2016-00034] Funding text: We are grateful to the Hungarian Research Foundation (OTKA No. K 115731). The financial support of the GINOP-2.3.2-15-2016-00014 and GINOP-2.3.2-15-2016-00034 projects are acknowledged. This work was partially supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences and by the Bolyai + New National Excellence Program (grant number: UNKP-18-4-SE-121) of the Ministry of Human Capacities (S. Beni). Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Szeged, H-6720, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University Hgyes, Endre u. 7., Budapest, H-1092, Hungary Servier Research Institute of Medicinal Chemistry (SRIMC), Záhony utca 7., Budapest, H-1031, Hungary Department of Pharmacognosy, Faculty of Pharmacy, Semmelweis University, Ülli út 26., Budapest, H-1085, Hungary Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary Department of Medical Chemistry, University of Szeged, Dóm t. 8., Szeged, H-6720, Hungary MTA SZTE Biomimetic Systems Research Group, Dóm t. 8., Szeged, H-6720, Hungary MTA TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary Cited By :4 Export Date: 25 July 2020 CODEN: CHCOF Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Hungary; email: fulop@pharm.u-szeged.hu CAplus AN 2019:196581; MEDLINE PMID: 30720807 (Journal; Article); Institute of Pharmaceutical Chemistry, University of Szeged, Eötvös u. 7., Szeged, H-6720, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University Hgyes, Endre u. 7., Budapest, H-1092, Hungary Servier Research Institute of Medicinal Chemistry (SRIMC), Záhony utca 7., Budapest, H-1031, Hungary Department of Pharmacognosy, Faculty of Pharmacy, Semmelweis University, Ülli út 26., Budapest, H-1085, Hungary Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary Department of Medical Chemistry, University of Szeged, Dóm t. 8., Szeged, H-6720, Hungary MTA SZTE Biomimetic Systems Research Group, Dóm t. 8., Szeged, H-6720, Hungary MTA TTK Lendület Artificial Transporter Research Group, Institute of Materials and Environmental Chemistry, Research Center for Natural Sciences, Hungarian Academy of Sciences Magyar, Tudósok krt. 2., Budapest, H-1117, Hungary Cited By :7 Export Date: 11 July 2021 CODEN: CHCOF Correspondence Address: Fülöp, F.; Institute of Pharmaceutical Chemistry, Eötvös u. 7., Hungary; email: fulop@pharm.u-szeged.hu AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Simon, Matthieu AU - Milbeo, Pierre AU - Liu, Hongtao AU - Andre, Christophe AU - Wenger, Emmanuel AU - Martinez, Jean AU - Amblard, Muriel AU - Aubert, Emmanuel AU - Legrand, Baptiste AU - Calmes, Monique TI - 12/10-Helix in Mixed beta-Peptides Alternating Bicyclic and Acyclic beta-Amino Acids: Probing the Relationship between Bicyclic Side Chain and Helix Stability JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 24 PY - 2018 IS - 70 SP - 18795 EP - 18800 PG - 6 SN - 0947-6539 DO - 10.1002/chem.201804404 UR - https://m2.mtmt.hu/api/publication/30378683 ID - 30378683 N1 - Institut des Biomolécules Max Mousseron (IBMM) UMR 5247, CNRS-Université Montpellier-ENSCM, Montpellier cedex 5, 34093, France CRM2, UMR 7063 CNRS Université de Lorraine, Boulevard des Aiguilletes, Vandoeuvre-lès-Nancy Cedex, 54506, France Cited By :1 Export Date: 6 March 2024 CODEN: CEUJE Correspondence Address: Legrand, B.; Institut des Biomolécules Max Mousseron (IBMM) UMR 5247, France; email: baptiste.legrand@umontpellier.fr AB - 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. LA - English DB - MTMT ER - TY - JOUR AU - Hogeweg, Anna AU - Sowislok, Andrea AU - Schrader, Thomas AU - Beuck, Christine TI - An NMR Method To Pinpoint Supramolecular Ligand Binding to Basic Residues on Proteins JF - ANGEWANDTE CHEMIE-INTERNATIONAL EDITION J2 - ANGEW CHEM INT EDIT VL - 56 PY - 2017 IS - 46 SP - 14758 EP - 14762 PG - 5 SN - 1433-7851 DO - 10.1002/anie.201707950 UR - https://m2.mtmt.hu/api/publication/27106548 ID - 27106548 N1 - University of Duisburg-Essen, Structural and Medicinal Biochemistry, Universitätsstrasse 2–5, Essen, 45144, Germany Bayer Pharma AG, Aprather Weg 18a, Wuppertal, 42096, Germany University of Duisburg-Essen, Organic Chemistry, Universitätsstrasse 2–5, Essen, 45144, Germany Cited By :17 Export Date: 8 September 2023 CODEN: ACIEF Correspondence Address: Beuck, C.; University of Duisburg-Essen, Universitätsstrasse 2–5, Germany; email: christine.beuck@uni-due.de LA - English DB - MTMT ER - TY - JOUR AU - Zhang, Yang AU - Xie, Sheng AU - Yan, Mingdi AU - Ramstroem, Olof TI - Dynamic Covalent Chemistry of Aldehyde Enamines: Bi-III- and Sc-III-Catalysis of Amine-Enamine Exchange JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 23 PY - 2017 IS - 49 SP - 11908 EP - 11912 PG - 5 SN - 0947-6539 DO - 10.1002/chem.201702363 UR - https://m2.mtmt.hu/api/publication/26876392 ID - 26876392 N1 - Department of Chemistry, KTH-Royal Institute of Technology, Teknikringen 36, Stockholm, 10044, Sweden Department of Chemistry, University of Massachusetts Lowell, 1 University Ave., Lowell, MA 01854, United States Cited By :11 Export Date: 8 September 2023 CODEN: CEUJE Correspondence Address: Yan, M.; Department of Chemistry, Teknikringen 36, Sweden; email: mingdi@kth.se LA - English DB - MTMT ER -