TY - JOUR AU - Bartus, Éva AU - Hegedüs, Zsófia AU - Wéber, Edit AU - Csipak, Brigitta AU - Szakonyi, Gerda AU - Martinek, Tamás TI - De Novo Modular Development of a Foldameric Protein-Protein Interaction Inhibitor for Separate Hot Spots: A Dynamic Covalent Assembly Approach JF - CHEMISTRYOPEN J2 - CHEMISTRYOPEN VL - 6 PY - 2017 IS - 2 SP - 236 EP - 241 PG - 6 SN - 2191-1363 DO - 10.1002/open.201700012 UR - https://m2.mtmt.hu/api/publication/3213189 ID - 3213189 LA - English DB - MTMT ER - TY - JOUR AU - Cabrele, C AU - Martinek, Tamás AU - Reiser, O AU - Berlicki, Ł TI - Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry JF - JOURNAL OF MEDICINAL CHEMISTRY J2 - J MED CHEM VL - 57 PY - 2014 IS - 23 SP - 9718 EP - 9739 PG - 22 SN - 0022-2623 DO - 10.1021/jm5010896 UR - https://m2.mtmt.hu/api/publication/2817673 ID - 2817673 AB - The construction of bioactive peptides using β-amino acid-containing sequence patterns is a very promising strategy to obtain analogues that exhibit properties of high interest for medicinal chemistry applications. β-Amino acids have been shown to modulate the conformation, dynamics, and proteolytic susceptibility of native peptides. They can be either combined with α-amino acids by following specific patterns, which results in backbone architectures with well-defined orientations of the side chain functional groups, or assembled in de novo-designed bioactive β- or α,β-peptidic sequences. Such peptides display various biological functions, including antimicrobial activity, inhibition of protein-protein interactions, agonism/antagonism of GPCR ligands, and anti-angiogenic activity. LA - English DB - MTMT ER - TY - JOUR AU - Mándity, István AU - Monsignori, A AU - Fülöp, Lívia AU - Forró, Enikő AU - Fülöp, Ferenc TI - Exploiting aromatic interactions for β-peptide foldamer helix stabilization: A significant design element JF - CHEMISTRY-A EUROPEAN JOURNAL J2 - CHEM-EUR J VL - 20 PY - 2014 IS - 16 SP - 4591 EP - 4597 PG - 7 SN - 0947-6539 DO - 10.1002/chem.201304448 UR - https://m2.mtmt.hu/api/publication/2583563 ID - 2583563 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 - Martinek, Tamás AU - Fülöp, Ferenc TI - Peptidic foldamers: ramping up diversity JF - CHEMICAL SOCIETY REVIEWS J2 - CHEM SOC REV VL - 41 PY - 2012 IS - 2 SP - 687 EP - 702 PG - 16 SN - 0306-0012 DO - 10.1039/c1cs15097a UR - https://m2.mtmt.hu/api/publication/1842290 ID - 1842290 N1 - Funding Agency and Grant Number: Hungarian Research FoundationOrszagos Tudomanyos Kutatasi Alapprogramok (OTKA) [NK81371, K83882, TAMOP-4.2.1/B-09/1/KONV-2010-0005]; COSTEuropean Cooperation in Science and Technology (COST) [CM0803]; Janos Bolyai FellowshipHungarian Academy of Sciences; HAS [LP2011-009/2011] Funding text: We thank the Hungarian Research Foundation (NK81371 and K83882), TAMOP-4.2.1/B-09/1/KONV-2010-0005 and COST (CM0803) for financial support. T.A.M. acknowledges the Janos Bolyai Fellowship and the "Lendulet'' programme (LP2011-009/2011) from the HAS. CAplus AN 2012:19612; MEDLINE PMID: 21769415 (Journal; General Review; Article; Research Support, Non-U.S. Gov't; Review); AB - Non-natural folded polymers (foldamers) display considerable versatility, and the design of such molecules is of great current interest. In this respect, peptidic foldamers are perhaps the best-characterized systems, as they populate a number of residue-controlled secondary structures, which have found various biological applications and have also led to the creation of nanostructured materials. This critical review covers recent developments related to diverse building blocks and modern foldamer design principles, such as the stereochemical patterning methods. The recent achievements concerning tertiary/quaternary structures and the self-assembling foldameric nanostructures are also addressed (176 references). 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 - Mándity, István AU - Fülöp, Lívia AU - Vass, Elemér AU - Tóth, Gábor AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly JF - ORGANIC LETTERS J2 - ORG LETT VL - 12 PY - 2010 IS - 23 SP - 5584 EP - 5587 PG - 4 SN - 1523-7060 DO - 10.1021/ol102494m UR - https://m2.mtmt.hu/api/publication/1412123 ID - 1412123 AB - The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter. 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 - Mándity, István AU - Fülöp, Lívia AU - Tóth, Gábor AU - Vass, Elemér AU - Hollósi, Miklós AU - Forró, Enikő AU - Fülöp, Ferenc TI - Effects of the alternating backbone configuration on the secondary structure and self-assembly of beta-peptides JF - JOURNAL OF THE AMERICAN CHEMICAL SOCIETY J2 - J AM CHEM SOC VL - 128 PY - 2006 IS - 41 SP - 13539 EP - 13544 PG - 6 SN - 0002-7863 DO - 10.1021/ja063890c UR - https://m2.mtmt.hu/api/publication/1078988 ID - 1078988 AB - Heterochiral homo-oligomers with alternating backbone configurations were constructed by using the different enantiomers of the cis- and trans-2-aminocyclopentanecarboxylic acid (ACPC) monomers. Molecular modeling and the spectroscopic techniques (NMR, ECD, and VCD) unequivocally proved that the alternating heterochiral cis-ACPC sequences form an H10/12 helix, where extra stabilization can be achieved via the cyclic side chains. The ECD and TEM measurements, together with molecular modeling, revealed that the alternating heterochiral trans-ACPC oligomers tend to attain a polar-strand secondary structure in solution, which can self-assemble into nanostructured fibrils. The observations indicate that coverage of all the possible secondary structures (various helix types and strand-mimicking conformations) can be attained with the help of cyclic beta-amino acid diastereomers. A relationship has been established between the backbone chirality pattern and the prevailing secondary structure, which underlines the role of stereochemical control in the beta-peptide secondary structure design and may contribute to future biological applications. LA - English DB - MTMT ER - TY - JOUR AU - Martinek, Tamás AU - Fülöp, Ferenc TI - Side-chain control of beta-peptide secondary structures - Design principles JF - EUROPEAN JOURNAL OF BIOCHEMISTRY J2 - EUR J BIOCHEM VL - 270 PY - 2003 IS - 18 SP - 3657 EP - 3666 PG - 10 SN - 0014-2956 DO - 10.1046/j.1432-1033.2003.03756.x UR - https://m2.mtmt.hu/api/publication/1013519 ID - 1013519 N1 - Cited By :147 Export Date: 27 September 2021 CODEN: EJBCA Correspondence Address: Fülöp, F.; Inst. of Pharmaceutical Chemistry, Eotvos u. 6, Szeged, Hungary; email: fulop@pharma.szote.u-szeged.hu Chemicals/CAS: Amino Acids; Peptides; Solvents AB - As one of the most important families of non-natural polymers with the propensity to form well-defined secondary structures, the beta-peptides are attracting increasing attention. The compounds incorporating beta-amino acid residues have found various applications in medicinal chemistry and biochemistry. The conformational pool of beta-peptides comprises several periodic folded conformations, which can be classified as helices, and nonpolar and polar strands. The latter two are prone to form pleated sheets. The numerous studies that have been performed on the side-chain dependence of the stability of the folded structures allow certain conclusions concerning the principles of design of the beta-peptide foldamers. The folding propensity is influenced by local torsional, side-chain to backbone and long-range side-chain interactions. Although beta-peptide foldamers are sensitive to solvent, the systematic choice of the side-chain pattern and spatiality allows the design of the desired specific secondary structure. The application of beta-peptide foldamers may open up new directions in the synthesis of highly organized artificial tertiary structures with biochemical functions. LA - English DB - MTMT ER -