@article{MTMT:3213189,
	title = {De Novo Modular Development of a Foldameric Protein-Protein Interaction Inhibitor for Separate Hot Spots: A Dynamic Covalent Assembly Approach},
	url = {https://m2.mtmt.hu/api/publication/3213189},
	author = {Bartus, Éva and Hegedüs, Zsófia and Wéber, Edit and Csipak, Brigitta and Szakonyi, Gerda and Martinek, Tamás},
	doi = {10.1002/open.201700012},
	journal-iso = {CHEMISTRYOPEN},
	journal = {CHEMISTRYOPEN},
	volume = {6},
	unique-id = {3213189},
	issn = {2191-1363},
	keywords = {FOLDAMERS; MOLECULAR RECOGNITION; PEPTIDOMIMETICS; protein–protein interactions; dynamic covalent chemistry},
	year = {2017},
	eissn = {2191-1363},
	pages = {236-241},
	orcid-numbers = {Bartus, Éva/0000-0001-9976-6978; Hegedüs, Zsófia/0000-0002-5546-8167; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Gerda/0000-0002-4366-4283; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2817673,
	title = {Peptides containing β-amino acid patterns: Challenges and successes in medicinal chemistry},
	url = {https://m2.mtmt.hu/api/publication/2817673},
	author = {Cabrele, C and Martinek, Tamás and Reiser, O and Berlicki, Ł},
	doi = {10.1021/jm5010896},
	journal-iso = {J MED CHEM},
	journal = {JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {57},
	unique-id = {2817673},
	issn = {0022-2623},
	abstract = {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.},
	year = {2014},
	eissn = {1520-4804},
	pages = {9718-9739},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:2583563,
	title = {Exploiting aromatic interactions for β-peptide foldamer helix stabilization: A significant design element},
	url = {https://m2.mtmt.hu/api/publication/2583563},
	author = {Mándity, István and Monsignori, A and Fülöp, Lívia and Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1002/chem.201304448},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {20},
	unique-id = {2583563},
	issn = {0947-6539},
	year = {2014},
	eissn = {1521-3765},
	pages = {4591-4597},
	orcid-numbers = {Mándity, István/0000-0003-2865-6143; Fülöp, Lívia/0000-0002-8010-0129; Forró, Enikő/0000-0001-6796-3889; Fülöp, Ferenc/0000-0003-1066-5287}
}

@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:1155933,
	title = {Sculpting the beta-peptide foldamer H12 helix via a designed side-chain shape},
	url = {https://m2.mtmt.hu/api/publication/1155933},
	author = {Hetényi, Anasztázia and Szakonyi, Zsolt and Mándity, István and Szolnoki, Éva Tünde and Tóth, Gábor and Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1039/b812114a},
	journal-iso = {CHEM COMMUN},
	journal = {CHEMICAL COMMUNICATIONS},
	unique-id = {1155933},
	issn = {1359-7345},
	abstract = {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.},
	keywords = {SECONDARY STRUCTURE; OLIGOMERS; AMINO-ACID; FORM},
	year = {2009},
	eissn = {1364-548X},
	pages = {177-179},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Szakonyi, Zsolt/0000-0003-2432-8409; Mándity, István/0000-0003-2865-6143; Tóth, Gábor/0000-0002-3604-4385; Martinek, Tamás/0000-0003-3168-8066; 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}
}

@article{MTMT:1013519,
	title = {Side-chain control of beta-peptide secondary structures - Design principles},
	url = {https://m2.mtmt.hu/api/publication/1013519},
	author = {Martinek, Tamás and Fülöp, Ferenc},
	doi = {10.1046/j.1432-1033.2003.03756.x},
	journal-iso = {EUR J BIOCHEM},
	journal = {EUROPEAN JOURNAL OF BIOCHEMISTRY},
	volume = {270},
	unique-id = {1013519},
	issn = {0014-2956},
	abstract = {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.},
	year = {2003},
	eissn = {1432-1033},
	pages = {3657-3666},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}