TY - THES AU - Szolnoki, Éva Tünde TI - β-Peptide foldamer helices with tailored diameters PB - Szegedi Tudományegyetem (SZTE) PY - 2018 SP - 59 DO - 10.14232/phd.9776 UR - https://m2.mtmt.hu/api/publication/3401999 ID - 3401999 LA - English DB - MTMT ER - TY - JOUR AU - Szolnoki, Éva Tünde AU - Hetényi, Anasztázia AU - Mándity, István AU - Fülöp, Ferenc AU - Martinek, Tamás TI - Foldameric β-H18/20P mixed helix stabilized by head-to-tail contacts: A way to higher-order structures Foldameric-H18/20P Mixed Helix Stabilized by Head-to-Tail Contacts: A Way to Higher-Order Structures JF - EUROPEAN JOURNAL OF ORGANIC CHEMISTRY J2 - EUR J ORG CHEM VL - 2013 PY - 2013 IS - 17 SP - 3555 EP - 3559 PG - 5 SN - 1434-193X DO - 10.1002/ejoc.201201633 UR - https://m2.mtmt.hu/api/publication/2347492 ID - 2347492 N1 - Funding Agency and Grant Number: European Union (EU) (COST Action) [CM0803]; Hungarian Research Foundation [OTKA PD83600, K83882]; Hungarian Academy of Sciences [LP-2011-009]; Gedeon Richter Centennial Foundation\n Funding text: This work was supported by the European Union (EU) (COST Action CM0803), the Hungarian Research Foundation (OTKA PD83600 and K83882), and the Hungarian Academy of Sciences (Lendulet programme, LP-2011-009). E. S. acknowleges support by the Gedeon Richter Centennial Foundation.\n WoS:hiba:000320036300015 2019-12-11 20:24 cím nem egyezik Funding Agency and Grant Number: European Union (EU) (COST Action)European Union (EU) [CM0803]; Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [OTKA PD83600, K83882]; Hungarian Academy of SciencesHungarian Academy of Sciences [LP-2011-009]; Gedeon Richter Centennial Foundation Funding text: This work was supported by the European Union (EU) (COST Action CM0803), the Hungarian Research Foundation (OTKA PD83600 and K83882), and the Hungarian Academy of Sciences (Lendulet programme, LP-2011-009). E. S. acknowleges support by the Gedeon Richter Centennial Foundation. AB - Peptidic foldamers are known to exhibit increased diversity in the periodic secondary-structure space in comparison with their natural counterparts, but their higher-order self-organization has been studied less thoroughly. In theory, large-diameter peptide foldamer helices have the capability of self-recognition through axial helix-helix interactions (e.g., head-to-tail), but this phenomenon has previously been observed in only one instance. In this article we report on the discovery of the largest-diameter β-peptidic mixed helix to date, the H18/20P helix. Its formation is solvent-dependent and its folding occurs cooperatively through head-to-tail self-assembly in solution. These findings suggest that axial helix-helix interactions can serve as a new mode for the formation of tertiary/quaternary structures for peptide foldamers, which also show higher-order structural diversity than natural proteins. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. LA - English DB - MTMT ER - TY - JOUR AU - Szolnoki, Éva Tünde AU - Hetényi, Anasztázia AU - Martinek, Tamás AU - Szakonyi, Zsolt AU - Fülöp, Ferenc TI - Self-association-driven transition of the β-peptidic H12 helix to the H18 helix JF - ORGANIC & BIOMOLECULAR CHEMISTRY J2 - ORG BIOMOL CHEM VL - 10 PY - 2012 IS - 2 SP - 255 EP - 259 PG - 5 SN - 1477-0520 DO - 10.1039/c1ob06627g UR - https://m2.mtmt.hu/api/publication/1842289 ID - 1842289 AB - Various patterns of foldameric oligomers formed by trans-ABHC ((1S,2S,3S, 5S)-2-amino-6,6-dimethylbicyclo-[3.3.1]heptane-3-carboxylic acid) and beta(3)-hSer residues were studied. NMR, ECD and molecular modelling demonstrated that octameric and nonameric sequences with multiple i-i+3 ABHC pair repulsions attain the beta-H18 helix in CD3OH. As a close relative of the alpha-helix, this helix type is stabilized by i-i+4 backbone H-bond interactions. The formation of the beta-H18 helix was found to be solvent-and concentration-dependent. Upon dilution, the beta-H18 -> beta-H12 helix transition was revealed by concentration-dependent ECD, DOSY-NMR and TEM measurements. LA - English DB - MTMT ER - TY - JOUR AU - Wéber, Edit AU - Hetényi, Anasztázia AU - Váczi, Balázs AU - Szolnoki, Éva Tünde AU - Fajka-Boja, Roberta AU - Tubak, Vilmos AU - Monostori, Éva AU - Martinek, Tamás TI - Galectin-1-Asialofetuin Interaction Is Inhibited by Peptides Containing the Tyr-Xxx-Tyr Motif Acting on the Glycoprotein JF - CHEMBIOCHEM J2 - CHEMBIOCHEM VL - 11 PY - 2010 IS - 2 SP - 228 EP - 234 PG - 7 SN - 1439-4227 DO - 10.1002/cbic.200900502 UR - https://m2.mtmt.hu/api/publication/1321061 ID - 1321061 N1 - Chemicals/CAS: galectin 1, 258495-34-0; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; Asialoglycoproteins; Galectin 1; Glycoproteins; Peptides; Recombinant Proteins; Tyrosine, 55520-40-6; alpha-Fetoproteins; asialofetuin Funding Agency and Grant Number: Hungarian Academy of Sciences; Hungarian Scientific Research Fund [K 69047, PD 75938]; NKTH-OTKA [CK 78188]; OTKA NF [69316]\n Funding text: A.H. and T.A.M. acknowledge the award of Janos Bolyai Research Fellowships by the Hungarian Academy of Sciences. This work was supported by grants from the Hungarian Scientific Research Fund (OTKA K 69047, PD 75938, NKTH-OTKA CK 78188, and OTKA NF 69316).\n AB - Galectin-1 (Gal-1), a ubiquitous P-galactoside-binding protein expressed by various normal and pathological tissues, has been implicated in cancer and autoimmune/inflammatory diseases in consequence of its regulatory role in adhesion, cell viability, proliferation, and angiogenesis. The functions of Gal-1 depend on its affinity for P-galactoside-containing glycoconjugates; accordingly, the inhibition of sugar binding blocks its functions, hence promising potential therapeutic tools. The Tyr-Xxx-Tyr peptide motifs have been reported to be glycomimetic sequences, mainly on the basis of their inhibitory effect on the Gal-1-asialofetuin (ASF) interaction. However, the results regarding the efficacy of the Tyr-Xxx-Tyr motif as a glycomimetic inhibitor are still controversial. The present STD and trNOE NMR experiments reveal that the Tyr-Xxx-Tyr peptides studied do not bind to Gal-1, whereas their binding to ASF is clearly detected. N-15,H-1 HSQC titrations with N-15-labeled Gal-1 confirm the absence of any peptide-Gal-1 interaction. These data indicate that the Tyr-Xxx-Tyr peptides tested in this work are not glycomimetics as they interact with ASF via an unrevealed molecular linkage. LA - English DB - MTMT ER - TY - JOUR AU - Hetényi, Anasztázia AU - Szakonyi, Zsolt AU - Mándity, István AU - Szolnoki, Éva Tünde AU - Tóth, Gábor AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape JF - CHEMICAL COMMUNICATIONS J2 - CHEM COMMUN PY - 2009 IS - 2 SP - 177 EP - 179 PG - 3 SN - 1359-7345 DO - 10.1039/b812114a UR - https://m2.mtmt.hu/api/publication/1155933 ID - 1155933 N1 - Funding Agency and Grant Number: Hungarian Research Foundation [NF69316, ALAP4-00092/2005]\n Funding text: We thank the Hungarian Research Foundation (OTKA No. NF69316) and ALAP4-00092/2005 for financial support. Z. S. and T. A. M. acknowledge the Janos Bolyai Fellowship from the HAS. We thank Dr Ilona Lacko for help with the ECD.\n CAplus AN 2008:1520260; MEDLINE PMID: 19099060 (Journal; Article; Research Support, Non-U.S. Gov't); AB - The long-range side-chain repulsion between the (1R, 2R, 3R, 5R)-2- amino-6,6-dimethyl-bicyclo[3.1.1]-heptane-3-carboxylic acid (trans-ABHC) residues stabilize the H12 helix in beta-peptide oligomers. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Szolnoki, Éva Tünde AU - Zalán, Zita AU - Fülöp, Ferenc TI - Synthesis And Steric Structure of Pyrrolidine- And Piperidine-fused 1,3,4,2-oxadiazaphosphinanes JF - ARKIVOC J2 - ARKIVOC VL - 2007 PY - 2007 IS - 5 SP - 202 EP - 209 PG - 8 SN - 1551-7012 DO - 10.3998/ark.5550190.0008.516 UR - https://m2.mtmt.hu/api/publication/1085086 ID - 1085086 N1 - Part number: 5 AB - Pyrrolidine- and piperidine-fused 1,3,4,2-oxadiazaphosphinane 2-oxides were prepared by cyclization of the corresponding pyrrolidine-and piperidine-hydrazino alcohols by using phosphorus-containing reagents. Stereochemical and conformational analyses were carried out in order to determine the effect of the ring size on the conformational behavior of the nitrogen-bridged bicyclic system. It was found that the chair conformation in the pyrrolidine-fused 1,3,4,2-oxadiazaphosphinane 2-oxides can be shifted toward twisted or distorted conformations. LA - English DB - MTMT ER -