TY - JOUR AU - El Battioui, Kamal AU - Chakraborty, Sohini AU - Wacha, András Ferenc AU - Molnár, Dániel AU - Quemé Peña, Mayra AU - Szigyártó, Imola Csilla AU - Szabó, Csenge Lilla AU - Bodor, Andrea AU - Horváti, Kata AU - Gyulai, Gergő AU - Bősze, Szilvia AU - Mihály, Judith AU - Jezsó, Bálint AU - Románszki, Loránd AU - Tóth, Judit AU - Varga, Zoltán AU - Mándity, István AU - Juhász, Tünde AU - Beke-Somfai, Tamás TI - In situ captured antibacterial action of membrane-incising peptide lamellae JF - NATURE COMMUNICATIONS J2 - NAT COMMUN VL - 15 PY - 2024 IS - 1 PG - 14 SN - 2041-1723 DO - 10.1038/s41467-024-47708-4 UR - https://m2.mtmt.hu/api/publication/34819821 ID - 34819821 N1 - Institute of Materials and Environmental Chemistry, HUN-REN Research Centre for Natural Sciences, Budapest, H-1117, Hungary Hevesy György Ph.D. School of Chemistry, Eötvös Loránd University, Budapest, H-1117, Hungary Institute of Molecular Life Sciences, HUN-REN Research Centre for Natural Sciences, Budapest, H-1117, Hungary Doctoral School of Biology and Institute of Biology, Eötvös Loránd University, Budapest, H-1117, Hungary ELTE Eötvös Loránd University, Institute of Chemistry, Analytical and BioNMR Laboratory, Budapest, H-1117, Hungary MTA-HUN-REN TTK “Momentum” Peptide-Based Vaccines Research Group, Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, H-1117, Hungary ELTE Eötvös Loránd University, Institute of Chemistry, Laboratory of Interfaces and Nanostructures, Budapest, H-1117, Hungary HUN-REN ELTE Research Group of Peptide Chemistry, Hungarian Research Network, Eötvös Loránd University, Budapest, Hungary ELTE-MTA “Momentum” Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest, Hungary Department of Applied Biotechnology and Food Sciences, Budapest University of Technology and Economics, Budapest, H-1111, Hungary Department of Physical Chemistry and Materials Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, Budapest, 1111, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University, Budapest, H-1092, Hungary Export Date: 8 May 2024 Correspondence Address: Beke-Somfai, T.; Institute of Materials and Environmental Chemistry, Hungary; email: beke-somfai.tamas@ttk.hu Chemicals/CAS: lysine, 56-87-1, 6899-06-5, 70-54-2; phosphate, 14066-19-4, 14265-44-2; Anti-Bacterial Agents; Lipopolysaccharides; Peptides Funding details: Eötvös Loránd Tudományegyetem, ELTE Funding details: Central European Institute of Technology, CEITEC Funding details: CZ.02.1.01/0.0/0.0/18_046/0015974 Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFIH, K142904, 2019-2.1.11-TÉT-2019-00091, SA-87/2021, K131594, 2020-1.1.2-PIACI-KFI-2020-00021, 144180, K137940, TKP2021-EGA-31, K138318, KEP-5/2021, K124900 Funding details: Magyar Tudományos Akadémia, MTA, NVKP_16-1-2016-0007, GINOP-2.3.2-15-2016-00017 Funding details: Ministerstvo Školství, Mládeže a Tělovýchovy, MŠMT, LM2023042, LM2018127 Funding text 1: This work was funded by the Momentum Program (LP2016-2 and LP2021-28) of the Hungarian Academy of Sciences, the National Competitiveness and Excellence Program (NVKP_16-1-2016-0007), the BIONANO_GINOP-2.3.2-15-2016-00017 project, and the National Research, Development and Innovation Office, Hungary (TKP2021-EGA-31, 2020-1.1.2-PIACI-KFI-2020-00021, 2019-2.1.11-T\\u00C9T-2019-00091, KKP_22 Project n.o. 144180, K131594 for J.M., K124900, K137940 for A.B., K142904 for Sz.B., and K138318 to J.T.). Support from E\\u00F6tv\\u00F6s Lor\\u00E1nd Research Network, Grant Nos. SA-87/2021 and KEP-5/2021, are also acknowledged. A.W. and Z.V. were supported by the J\\u00E1nos Bolyai Research Scholarship of the Hungarian Academy of Sciences. The authors acknowledge support from ELTE Thematic Excellence Programme 2020, the Szint+ Program, National Challenges Subprogramme-TKP2020-NKA-06. CIISB, Instruct-CZ Centre of Instruct-ERIC EU consortium, funded by MEYS CR infrastructure project LM2018127, LM2023042 and European Regional Development Fund-Project \\u201EUP CIISB\\u201C (No. CZ.02.1.01/0.0/0.0/18_046/0015974), is gratefully acknowledged for the financial support of the measurements at the CF Cryo-Electron Microscopy and Tomography. The authors thank Daniel Pinkas at CEITEC, Brno, for his excellent technical assistance and support. Fig. (inset), Fig. and Supplementary Fig. have been created with BioRender.com. Funding text 2: This work was funded by the Momentum Program (LP2016-2 and LP2021-28) of the Hungarian Academy of Sciences, the National Competitiveness and Excellence Program (NVKP_16-1-2016-0007), the BIONANO_GINOP-2.3.2-15-2016-00017 project, and the National Research, Development and Innovation Office, Hungary (TKP2021-EGA-31, 2020-1.1.2-PIACI-KFI-2020-00021, 2019-2.1.11-T\\u00C9T-2019-00091, KKP_22 Project n.o. 144180, K131594 for J.M., K124900, K137940 for A.B., K142904 for Sz.B., and K138318 to J.T.). Support from E\\u00F6tv\\u00F6s Lor\\u00E1nd Research Network, Grant Nos. SA-87/2021 and KEP-5/2021, are also acknowledged. A.W. and Z.V. were supported by the J\\u00E1nos Bolyai Research Scholarship of the Hungarian Academy of Sciences. The authors acknowledge support from ELTE Thematic Excellence Programme 2020, the Szint+ Program, National Challenges Subprogramme-TKP2020-NKA-06. CIISB, Instruct-CZ Centre of Instruct-ERIC EU consortium, funded by MEYS CR infrastructure project LM2018127, LM2023042 and European Regional Development Fund-Project \\u201EUP CIISB\\u201C (No. CZ.02.1.01/0.0/0.0/18_046/0015974), is gratefully acknowledged for the financial support of the measurements at the CF Cryo-Electron Microscopy and Tomography. The authors thank Daniel Pinkas at CEITEC, Brno, for his excellent technical assistance and support. Fig. 1b (inset), Fig. 2d and Supplementary Fig.\\u00A021 have been created with BioRender.com. AB - Developing unique mechanisms of action are essential to combat the growing issue of antimicrobial resistance. Supramolecular assemblies combining the improved biostability of non-natural compounds with the complex membrane-attacking mechanisms of natural peptides are promising alternatives to conventional antibiotics. However, for such compounds the direct visual insight on antibacterial action is still lacking. Here we employ a design strategy focusing on an inducible assembly mechanism and utilized electron microscopy (EM) to follow the formation of supramolecular structures of lysine-rich heterochiral β 3 -peptides, termed lamellin-2K and lamellin-3K, triggered by bacterial cell surface lipopolysaccharides. Combined molecular dynamics simulations, EM and bacterial assays confirmed that the phosphate-induced conformational change on these lamellins led to the formation of striped lamellae capable of incising the cell envelope of Gram-negative bacteria thereby exerting antibacterial activity. Our findings also provide a mechanistic link for membrane-targeting agents depicting the antibiotic mechanism derived from the in-situ formation of active supramolecules. LA - English DB - MTMT ER - TY - CONF AU - Tasvilla, Sonallya AU - Szigyártó, Imola Csilla AU - Juhász, Tünde AU - Edit, I. Buzas AU - Delaram, Khamari AU - Kinga, Ilyes AU - Varga, Zoltán AU - Beke-Somfai, Tamás TI - Systematic investigation and classification of membrane active peptide peptides based on their affinity for interaction with extracellular vesicles T2 - Small New World 2.0 PY - 2023 SP - 63 UR - https://m2.mtmt.hu/api/publication/34627971 ID - 34627971 LA - English DB - MTMT ER - TY - JOUR AU - Juhász, Tünde AU - Quemé Peña, Mayra AU - Beke-Somfai, Tamás TI - Unique thermophoretic behavior of supramolecular assemblies of cationic antimicrobial peptides with anionic small molecule agents JF - JOURNAL OF MOLECULAR LIQUIDS J2 - J MOL LIQ VL - 386 PY - 2023 PG - 11 SN - 0167-7322 DO - 10.1016/j.molliq.2023.122513 UR - https://m2.mtmt.hu/api/publication/34077467 ID - 34077467 N1 - Export Date: 15 November 2023 CODEN: JMLID Correspondence Address: Juhász, T.; Institute of Materials and Environmental Chemistry, Magyar tudósok körútja 2, Hungary; email: juhasz.tunde@ttk.hu LA - English DB - MTMT ER - TY - JOUR AU - Szeltner, Zoltán AU - Ferenc, Györgyi AU - Juhász, Tünde AU - Kupihár, Zoltán AU - Váradi, Zoltán AU - Szüts, Dávid AU - Kovács, Lajos TI - Probing telomeric-like G4 structures with full or partial 2′-deoxy-5-hydroxyuridine substitutions JF - BIOCHIMIE J2 - BIOCHIMIE VL - 214 PY - 2023 IS - Part A SP - 33 EP - 44 PG - 12 SN - 0300-9084 DO - 10.1016/j.biochi.2023.01.009 UR - https://m2.mtmt.hu/api/publication/33697937 ID - 33697937 N1 - Institute of Enzymology, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, Budapest, H-1117, Hungary Nucleic Acid Synthesis Laboratory, Biological Research Centre, Eötvös Loránd Research Network, Temesvári Krt. 62, Szeged, H-6726, Hungary Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, Budapest, H-1117, Hungary Department of Medicinal Chemistry, University of Szeged, Dom Tér 8, Szeged, H-6720, Hungary Export Date: 13 March 2023 CODEN: BICMB Correspondence Address: Szüts, D.; Institute of Enzymology, Magyar Tudósok Körútja 2, Hungary; email: szuts.david@ttk.hu Correspondence Address: Kovács, L.; Department of Medicinal Chemistry, Dom Tér 8, Hungary; email: kovacs.lajos@med.u-szeged-hu Funding details: Eötvös Loránd Tudományegyetem, ELTE Funding details: National Research, Development and Innovation Office, 2018–1.2.1-NKP-2018-00005, K128801 Funding text 1: We thank Mihály Kovács and Gábor Harami (ELTE) for supplying us with BLM helicase. This work was supported by the National Research Development and Innovation Office of Hungary (grants no. K128801 and 2018–1.2.1-NKP-2018-00005 ). Funding text 2: We thank Mihály Kovács and Gábor Harami (ELTE) for supplying us with BLM helicase. This work was supported by the National Research Development and Innovation Office of Hungary (grants no. K128801 and 2018–1.2.1-NKP-2018-00005). AB - Guanine quadruplexes (G4s) are stable four-stranded secondary DNA structures held together by noncanonical G-G base tetrads. We synthesised the nucleoside analogue 2′-deoxy-5-hydroxyuridine (H) and inserted its phosphoramidite into telomeric repeat-type model oligonucleotides. Full and partial substitutions were made, replacing all guanines in all the three tetrads of a three-tier G4 structure, or only in the putative upper, central, or lower tetrads. We characterised these modified structures using CD, UV absorbance spectroscopy, native gel studies, and a capture oligo-based G4 disruption kinetic assay. The strand separation activity of BLM helicase on these substituted structures was also investigated. Two of the partially H-substituted constructs adopted G4-like structures, but displayed lower thermal stabilities compared to unsubstituted G4. The construct modified in its central tetrad remained mostly denatured, but the possibility of a special structure for the fully replaced variant remained open. H substitutions did not interfere with the G4-resolving activity of BLM helicase, but its efficiency was highly influenced by construct topology and even more by the G4 ligand PhenDC3. Our results suggest that the H modification can be incorporated into G quadruplexes, but only at certain positions to maintain G4 stability. The destabilizing effect observed for 2′-deoxy-5-hydroxyuridine indicates that the cytosine deamination product 5-hydroxyuracil and its nucleoside counterpart in RNA (5-hydroxyuridine), might also be destabilizing in cellular DNA and RNA quadruplexes. The kinetic assay employed in this study can be generally employed for a fast comparison of the stabilities of various G4s either in their free or ligand-bound states. © 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM) LA - English DB - MTMT ER - TY - JOUR AU - Dürvanger, Zsolt AU - Juhász, Tünde AU - Liliom, Károly AU - Harmat, Veronika TI - Structures of calmodulin-melittin complexes show multiple binding modes lacking classical anchoring interactions JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 299 PY - 2023 IS - 4 PG - 15 SN - 0021-9258 DO - 10.1016/j.jbc.2023.104596 UR - https://m2.mtmt.hu/api/publication/33696970 ID - 33696970 N1 - Export Date: 2 June 2023 CODEN: JBCHA Correspondence Address: Harmat, V.; Laboratory of Structural Chemistry and Biology, Hungary; email: veronika.harmat@ttk.elte.hu AB - Calmodulin (CaM) is a Ca2+ sensor protein found in all eukaryotic cells that regulates a large number of target proteins in a Ca2+ concentration-dependent manner. As a transient type hub protein, it recognizes linear motifs of its targets, though for the Ca2+-dependent binding no consensus sequence was identified. Its complex with melittin, a major component of bee venom, is often used as a model system of protein - protein complexes. Yet, the structural aspects of the binding are not well understood, as only diverse, low-resolution data are available concerning the association. We present the crystal structure of melittin in complex with Ca2+-saturated calmodulins from two, evolutionarily distant species, Homo sapiens and Plasmodium falciparum representing three binding modes of the peptide. Results - augmented by molecular dynamics simulations - indicate that multiple binding modes can exist for CaM-melittin complexes, as an intrinsic characteristic of the binding. While the helical structure of melittin remains, swapping of its salt bridges and partial unfolding of its C-terminal segment can occur. In contrast to the classical way of target recognition by CaM, we found that different sets of residues can anchor at the hydrophobic pockets of CaM, which were considered as main recognition sites. Finally, the nanomolar binding affinity of the CaM-melittin complex is created by an ensemble of arrangements of similar stability - tight binding is achieved not by optimized specific interactions but by simultaneously satisfying less optimal interaction patterns in co-existing different conformers. LA - English DB - MTMT ER - TY - JOUR AU - Bóta, Attila AU - Fehér, Bence AU - Wacha, András Ferenc AU - Juhász, Tünde AU - Szabó, Dániel AU - Turiák, Lilla AU - Gaál, Anikó AU - Varga, Zoltán AU - Amenitsch, Heinz AU - Mihály, Judith TI - Lipid nanoparticles with erythrocyte cell-membrane proteins JF - JOURNAL OF MOLECULAR LIQUIDS J2 - J MOL LIQ VL - 369 PY - 2023 PG - 10 SN - 0167-7322 DO - 10.1016/j.molliq.2022.120791 UR - https://m2.mtmt.hu/api/publication/33298558 ID - 33298558 N1 - CODEN: JMLID LA - English DB - MTMT ER - TY - JOUR AU - Udyavara Nagaraj, Vignesh AU - Juhász, Tünde AU - Quemé Peña, Mayra AU - Szigyártó, Imola Csilla AU - Bogdán, Dóra AU - Wacha, András Ferenc AU - Mihály, Judith AU - Románszki, Loránd AU - Varga, Zoltán AU - Andréasson, Joakim AU - Mándity, István AU - Beke-Somfai, Tamás TI - Stimuli-Responsive Membrane Anchor Peptide Nanofoils for Tunable Membrane Association and Lipid Bilayer Fusion JF - ACS APPLIED MATERIALS & INTERFACES J2 - ACS APPL MATER INTER VL - 14 PY - 2022 IS - 50 SP - 55320 EP - 55331 PG - 12 SN - 1944-8244 DO - 10.1021/acsami.2c11946 UR - https://m2.mtmt.hu/api/publication/33369174 ID - 33369174 N1 - Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, H-1117, Hungary Hevesy György Ph.D. School of Chemistry, Eötvös Loránd University, Budapest, H-1117, Hungary Department of Organic Chemistry, Faculty of Pharmacy, Semmelweis University, Budapest, H-1092, Hungary Department of Chemistry and Chemical Engineering, Physical Chemistry, Chalmers University of Technology, Gothenburg, SE-412 96, Sweden Cited By :2 Export Date: 15 November 2023 Correspondence Address: Beke-Somfai, T.; Institute of Materials and Environmental Chemistry, Hungary; email: beke-somfai.tamas@ttk.hu LA - English DB - MTMT ER - TY - JOUR AU - Udyavara Nagaraj, Vignesh AU - Juhász, Tünde AU - Quemé Peña, Mayra AU - Szigyártó, Imola Csilla AU - Bogdán, Dóra AU - Wacha, András Ferenc AU - Mihály, Judith AU - Románszki, Loránd AU - Varga, Zoltán AU - Mándity, István AU - Beke-Somfai, Tamás TI - Sel-assembled Peptide Bilayer for Photo-reversible Association on Lipid Membranes JF - JOURNAL OF PEPTIDE SCIENCE J2 - J PEPT SCI VL - 28 PY - 2022 IS - Suppl.3. SN - 1075-2617 DO - 10.1002/psc.3445 UR - https://m2.mtmt.hu/api/publication/33191148 ID - 33191148 LA - English DB - MTMT ER - TY - JOUR AU - Tóth, Vilmos AU - Vadászi, Henrietta AU - Ravasz, Lilla AU - Mittli, Dániel Árpád AU - Mátyás, Dominik AU - Molnár, Tamás AU - Micsonai, András AU - Szaniszló, Tamás AU - Lőrincz, Péter AU - Kovács, Réka AU - Juhász, Tünde AU - Beke-Somfai, Tamás AU - Juhász, Gábor Dénes AU - Györffy, Balázs AU - Kékesi, Adrienna Katalin AU - Kardos, József TI - Neuronal-specific septin-3 binds Atg8/LC3B, accumulates and localizes to autophagosomes during induced autophagy JF - CELLULAR AND MOLECULAR LIFE SCIENCES J2 - CELL MOL LIFE SCI VL - 79 PY - 2022 IS - 9 PG - 18 SN - 1420-682X DO - 10.1007/s00018-022-04488-8 UR - https://m2.mtmt.hu/api/publication/33053520 ID - 33053520 N1 - ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary Department of Biochemistry, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary Institute of Materials and Environmental Chemistry, Research Centre for Natural Sciences, Budapest, Hungary CRU Hungary Ltd., Göd, Hungary Department of Neuroscience, University of Copenhagen, Copenhagen, Denmark Department of Physiology and Neurobiology, Eötvös Loránd University, Budapest, Hungary Laboratory of Proteomics, Institute of Biology, ELTE Eötvös Loránd University, Budapest, Hungary Export Date: 21 September 2022 CODEN: CMLSF Correspondence Address: Kardos, J.; ELTE NAP Neuroimmunology Research Group, Hungary; email: kardos@elte.hu AB - In synapses that show signs of local apoptosis and mitochondrial stress and undergo neuro-immunological synapse pruning, an increase in the levels of the presynaptic protein, neuronal-specific septin-3 can be observed. Septin-3 is a member of the septin GTPase family with the ability to form multimers and contribute to the cytoskeleton. However, the function of septin-3 remains elusive. Here, we provide evidence that septin-3 is capable of binding the most-studied autophagy protein Atg8 homolog microtubule-associated protein 1 light chain 3B (LC3B), besides another homolog, GABA receptor-associated protein-like 2 (GABARAPL2). Moreover, we demonstrate that colocalization of septin-3 and LC3B increases upon chemical autophagy induction in primary neuronal cells. Septin-3 is accumulated in primary neurons upon autophagy enhancement or blockade, similar to autophagy proteins. Using electron microscopy, we also show that septin-3 localizes to LC3B positive membranes and can be found at mitochondria. However, colocalization results of septin-3 and the early mitophagy marker PTEN-induced kinase 1 (PINK1) do not support that binding of septin-3 to mitochondria is mitophagy related. We conclude that septin-3 correlates with synaptic/neuronal autophagy, binds Atg8 and localizes to autophagic membranes that can be enhanced with chemical autophagy induction. Based on our results, elevated septin-3 levels might indicate enhanced or impeded autophagy in neurons. LA - English DB - MTMT ER - TY - JOUR AU - Petri, László AU - Ábrányi-Balogh, Péter AU - Vagrys, Darius AU - Imre, Timea AU - Varró, Nikolett AU - Mándity, István AU - Rácz, Anita AU - Wittner, Lucia AU - Tóth, Kinga AU - Tóth, Estilla Zsófia AU - Juhász, Tünde AU - Davis, Ben AU - Keserű, György Miklós TI - A covalent strategy to target intrinsically disordered proteins: Discovery of novel tau aggregation inhibitors JF - EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY J2 - EUR J MED CHEM VL - 231 PY - 2022 PG - 13 SN - 0223-5234 DO - 10.1016/j.ejmech.2022.114163 UR - https://m2.mtmt.hu/api/publication/32649994 ID - 32649994 LA - English DB - MTMT ER -