@article{MTMT:2459240,
	title = {Foldameric α/β-Peptide Analogs of the β-Sheet-Forming Antiangiogenic Anginex: Structure and Bioactivity},
	url = {https://m2.mtmt.hu/api/publication/2459240},
	author = {Hegedüs, Zsófia and Wéber, Edit and Kriston-Pál, Éva and Makra, Ildikó and Czibula, Ágnes and Monostori, Éva and Martinek, Tamás},
	doi = {10.1021/ja408054f},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {135},
	unique-id = {2459240},
	issn = {0002-7863},
	abstract = {The principles of beta-sheet folding and design for alpha-peptidic sequences are well established, while those for sheet mimetics containing homologated amino acid building blocks are still under investigation. To reveal the structure-function relations of beta-amino-acid-containing foldamers, we followed a top-down approach to study a series of alpha/beta-peptidic analogs of anginex, a beta-sheet-forming antiangiogenic peptide. Eight anginex analogs were developed by systematic alpha --> beta(3) substitutions and analyzed by using NMR and CD spectroscopy. The foldamers retained the beta-sheet tendency, though with a decreased folding propensity. beta-Sheet formation could be induced by a micellar environment, similarly to that of the parent peptide. The destructuring effect was higher when the alpha --> beta(3) exchange was located in the beta-sheet core. Analysis of the beta-sheet stability versus substitution pattern and the local conformational bias of the bulky beta(3)V and beta(3)I residues revealed that a mismatch between the H-bonding preferences of the alpha- and beta-residues played a minor role in the structure-breaking effect. Temperature-dependent CD and NMR measurements showed that the hydrophobic stabilization was scaled-down for the alpha/beta-peptides. Analysis of the biological activity of the foldamer peptides showed that four anginex derivatives dose-dependently inhibited the proliferation of a mouse endothelial cell line. The alpha --> beta(3) substitution strategy applied in this work can be a useful approach to the construction of bioactive beta-sheet mimetics with a reduced aggregation tendency and improved pharmacokinetic properties.},
	year = {2013},
	eissn = {1520-5126},
	pages = {16578-16584},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Czibula, Ágnes/0000-0003-4461-2773; Monostori, Éva/0000-0002-7442-3562; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2347492,
	title = {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},
	url = {https://m2.mtmt.hu/api/publication/2347492},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Mándity, István and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/ejoc.201201633},
	journal-iso = {EUR J ORG CHEM},
	journal = {EUROPEAN JOURNAL OF ORGANIC CHEMISTRY},
	volume = {2013},
	unique-id = {2347492},
	issn = {1434-193X},
	abstract = {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.},
	keywords = {PEPTIDES; FOLDAMERS; Protein Folding; amino acids; self-assembly; helical structures},
	year = {2013},
	eissn = {1099-0690},
	pages = {3555-3559},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1842290,
	title = {Peptidic foldamers: ramping up diversity},
	url = {https://m2.mtmt.hu/api/publication/1842290},
	author = {Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/c1cs15097a},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {41},
	unique-id = {1842290},
	issn = {0306-0012},
	abstract = {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).},
	keywords = {DE-NOVO DESIGN; BETA-AMINO ACIDS; PROTEINOGENIC SIDE-CHAINS; MODEL SYNTHETIC FOLDAMERS; GCN4 LEUCINE-ZIPPER; HYDROGEN-BONDED RINGS; PARALLEL SHEET STRUCTURE; MIXED ALPHA/BETA-PEPTIDES; HELICAL SECONDARY STRUCTURES; EFFECTIVE SIMULATION PROTOCOLS},
	year = {2012},
	eissn = {1460-4744},
	pages = {687-702},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1842289,
	title = {Self-association-driven transition of the β-peptidic H12 helix to the H18 helix},
	url = {https://m2.mtmt.hu/api/publication/1842289},
	author = {Szolnoki, Éva Tünde and Hetényi, Anasztázia and Martinek, Tamás and Szakonyi, Zsolt and Fülöp, Ferenc},
	doi = {10.1039/c1ob06627g},
	journal-iso = {ORG BIOMOL CHEM},
	journal = {ORGANIC & BIOMOLECULAR CHEMISTRY},
	volume = {10},
	unique-id = {1842289},
	issn = {1477-0520},
	abstract = {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.},
	keywords = {SECONDARY STRUCTURE; CIRCULAR-DICHROISM; SIDE-CHAINS; ACID OLIGOMERS; QUATERNARY STRUCTURE; ALPHA/BETA-PEPTIDES; STRUCTURAL-CHARACTERIZATION; AMPHIPATHIC PEPTIDES; MEMBRANE ENVIRONMENT; HETEROGENEOUS BACKBONES},
	year = {2012},
	eissn = {1477-0539},
	pages = {255-259},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Martinek, Tamás/0000-0003-3168-8066; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1412123,
	title = {Building β-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly},
	url = {https://m2.mtmt.hu/api/publication/1412123},
	author = {Mándity, István and Fülöp, Lívia and Vass, Elemér and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1021/ol102494m},
	journal-iso = {ORG LETT},
	journal = {ORGANIC LETTERS},
	volume = {12},
	unique-id = {1412123},
	issn = {1523-7060},
	abstract = {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.},
	keywords = {ASSOCIATION; FAMILY; DESIGN; SECONDARY STRUCTURE; NMR; OLIGOMERS; amino acids; CD; LYOTROPIC LIQUID-CRYSTALS},
	year = {2010},
	eissn = {1523-7052},
	pages = {5584-5587},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Vass, Elemér/0000-0001-8898-3846; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1232853,
	title = {Design of Peptidic Foldamer Helices: A Stereochemical Patterning Approach},
	url = {https://m2.mtmt.hu/api/publication/1232853},
	author = {Mándity, István and Wéber, Edit and Martinek, Tamás and Olajos, Gábor and Tóth, Gábor and Vass, Elemér and Fülöp, Ferenc},
	doi = {10.1002/anie.200805095},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {48},
	unique-id = {1232853},
	issn = {1433-7851},
	keywords = {SEQUENCES; SECONDARY STRUCTURE; CONFORMATIONS; DE-NOVO DESIGN; PROTEINOGENIC SIDE-CHAINS; FOLDAMERS; OLIGOMERS; amino acids; NMR spectroscopy; ALPHA/BETA-PEPTIDES; helical structures; BETA-AMINO-ACID; BETA(3)-PEPTIDES},
	year = {2009},
	eissn = {1521-3773},
	pages = {2171-2175},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Wéber, Edit/0000-0002-5904-0619; Martinek, Tamás/0000-0003-3168-8066; Olajos, Gábor/0000-0002-2479-4891; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Fülöp, Ferenc/0000-0003-1066-5287}
}

@article{MTMT:1078988,
	title = {Effects of the alternating backbone configuration on the secondary structure and self-assembly of beta-peptides},
	url = {https://m2.mtmt.hu/api/publication/1078988},
	author = {Martinek, Tamás and Mándity, István and Fülöp, Lívia and Tóth, Gábor and Vass, Elemér and Hollósi, Miklós and Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1021/ja063890c},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {128},
	unique-id = {1078988},
	issn = {0002-7863},
	abstract = {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.},
	keywords = {SIDE-CHAINS; FOLDAMERS; OLIGOMERS; DESIGN PRINCIPLES; AMINO-ACID; CHIRAL MOLECULES; VIBRATIONAL CIRCULAR-DICHROISM; SHORT ALPHA/BETA-PEPTIDES; HELICAL CONFORMATIONS},
	year = {2006},
	eissn = {1520-5126},
	pages = {13539-13544},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}