@article{MTMT:2868602,
	title = {Induced Folding of Protein-Sized Foldameric β-Sandwich Models with Core β-Amino Acid Residues},
	url = {https://m2.mtmt.hu/api/publication/2868602},
	author = {Olajos, Gábor and Hetényi, Anasztázia and Wéber, Edit and Németh, Lukács and Szakonyi, Zsolt and Fülöp, Ferenc and Martinek, Tamás},
	doi = {10.1002/chem.201405581},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {21},
	unique-id = {2868602},
	issn = {0947-6539},
	abstract = {The mimicry of protein-sized β-sheet structures with unnatural peptidic sequences (foldamers) is a considerable challenge. In this work, the de novo designed betabellin-14 β-sheet has been used as a template, and α→β residue mutations were carried out in the hydrophobic core (positions 12 and 19). β-Residues with diverse structural properties were utilized: Homologous β3-amino acids, (1R,2S)-2-aminocyclopentanecarboxylic acid (ACPC), (1R,2S)-2-aminocyclohexanecarboxylic acid (ACHC), (1R,2S)-2-aminocyclohex-3-enecarboxylic acid (ACEC), and (1S,2S,3R,5S)-2-amino-6,6-dimethylbicyclo[3.1.1]heptane-3-carboxylic acid (ABHC). Six α/β-peptidic chains were constructed in both monomeric and disulfide-linked dimeric forms. Structural studies based on circular dichroism spectroscopy, the analysis of NMR chemical shifts, and molecular dynamics simulations revealed that dimerization induced β-sheet formation in the 64-residue foldameric systems. Core replacement with (1R,2S)-ACHC was found to be unique among the β-amino acid building blocks studied because it was simultaneously able to maintain the interstrand hydrogen-bonding network and to fit sterically into the hydrophobic interior of the β-sandwich. The novel β-sandwich model containing 25% unnatural building blocks afforded protein-like thermal denaturation behavior. Dissolving sandwiches: A water-soluble β-sandwich has been constructed by using cyclic β-amino acids in the hydrophobic core (see figure). The structural stability is highly dependent on the side-chain, and the destructuring effects of the β-residues could be minimized by using (1R,2S)-2-aminocyclohexanecarboxylic acid. The β-sandwich displays protein-like thermal denaturation behavior.},
	keywords = {PROTEINS; STABILITY; Protein Folding; Chemical bonds; amino acids; PEPTIDOMIMETICS; DICHROISM; molecular dynamics; chemical analysis; DYES; Hydrophobicity; Hydrogen bonds; molecular dynamics simulations; CHAINS; circular dichroism spectroscopy; Structural stabilities; Protein Engineering; Thermal denaturations; Hydrogen bonding network; NMR chemical shifts; PROTEIN STRUCTURES},
	year = {2015},
	eissn = {1521-3765},
	pages = {6173-6180},
	orcid-numbers = {Olajos, Gábor/0000-0002-2479-4891; Hetényi, Anasztázia/0000-0001-8080-6992; Wéber, Edit/0000-0002-5904-0619; Szakonyi, Zsolt/0000-0003-2432-8409; Fülöp, Ferenc/0000-0003-1066-5287; 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:2764648,
	title = {Predicting Order and Disorder for β-Peptide Foldamers in Water},
	url = {https://m2.mtmt.hu/api/publication/2764648},
	author = {Németh, Lukács and Hegedüs, Zsófia and Martinek, Tamás},
	doi = {10.1021/ci5003476},
	journal-iso = {J CHEM INF MODEL},
	journal = {JOURNAL OF CHEMICAL INFORMATION AND MODELING},
	volume = {54},
	unique-id = {2764648},
	issn = {1549-9596},
	abstract = {Following a quantitative validation approach, we tested the AMBER ff03 and GAFF force fields with the TIP3P explicit water model in molecular dynamic simulations of beta-peptide foldamers. The test sequences were selected to represent a wide range of folding behavior in water: compact helix, strand mimetic geometry, and the state of disorder. The combination AMBER ff03-TIP3P successfully predicted the experimentally observed conformational properties and reproduced the NOE distances and backbone (3)J coupling data at a good level. GAFF was unable to produce folded structures correctly due to its biased torsion potentials. We can recommend AMBER ff03-TIP3P for simulations involving beta-peptide sequences in aqueous media including ordered and disordered structures.},
	year = {2014},
	eissn = {1549-960X},
	pages = {2776-2783},
	orcid-numbers = {Hegedüs, Zsófia/0000-0002-5546-8167; Martinek, Tamás/0000-0003-3168-8066}
}

@article{MTMT:1926671,
	title = {Unique α,β- and α,α,β,β-peptide foldamers based on cis-β-aminocyclopentanecarboxylic acid},
	url = {https://m2.mtmt.hu/api/publication/1926671},
	author = {Berlicki, Ł and Pilsl, L and Wéber, Edit and Mándity, István and Cabrele, C and Martinek, Tamás and Fülöp, Ferenc and Reiser, O},
	doi = {10.1002/anie.201107702},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {51},
	unique-id = {1926671},
	issn = {1433-7851},
	abstract = {Waterproof: cis-β-Aminocylopentanecarboxylic acid is a highly suitable building block for the synthesis of α,β- and α,α,β, β-peptides that have unique helical structures with high stability in methanol and aqueous media. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.},
	keywords = {PEPTIDES; METHANOL; FOLDAMERS; amino acids; helical structures; aqueous media; Building blockes; High stability; cis-pentacine; β-amino acids},
	year = {2012},
	eissn = {1521-3773},
	pages = {2208-2212},
	orcid-numbers = {Wéber, Edit/0000-0002-5904-0619; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Fülöp, Ferenc/0000-0003-1066-5287}
}

@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:1012938,
	title = {Application of alicyclic beta-amino acids in peptide chemistry},
	url = {https://m2.mtmt.hu/api/publication/1012938},
	author = {Fülöp, Ferenc and Martinek, Tamás and Tóth, Gábor},
	doi = {10.1039/B501173F},
	journal-iso = {CHEM SOC REV},
	journal = {CHEMICAL SOCIETY REVIEWS},
	volume = {35},
	unique-id = {1012938},
	issn = {0306-0012},
	abstract = {The self-organizing beta-peptides have attracted considerable interest in the fields of foldamer chemistry and biochemistry. These compounds exhibit various stable secondary structure motifs that can be exploited to construct biologically active substances and nanostructured tertiary structures. The secondary structures can be controlled via the beta-amino acid sequence, and cyclic beta-amino acid residues play a crucial role in the design. The most important procedures for the preparation of cyclic beta-amino acid monomers and peptides are discussed in this tutorial review. Besides the secondary structure design principles, the methods of folded structure detection are surveyed.},
	keywords = {DERIVATIVES; TRANSFORMATION; STEREOSELECTIVE-SYNTHESIS; HELIX; OLIGOMERS; DESIGN PRINCIPLES; TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID; SELF-ASSOCIATION; DESYMMETRIZATION},
	year = {2006},
	eissn = {1460-4744},
	pages = {323-334},
	orcid-numbers = {Fülöp, Ferenc/0000-0003-1066-5287; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385}
}