@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:1085087,
	title = {The First Direct Enzymatic Hydrolysis of Alicyclic Beta-amino Esters: A Route to Enantiopure Cis And Trans Beta-amino Acids},
	url = {https://m2.mtmt.hu/api/publication/1085087},
	author = {Forró, Enikő and Fülöp, Ferenc},
	doi = {10.1002/chem.200700257},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {13},
	unique-id = {1085087},
	issn = {0947-6539},
	abstract = {The first direct enzymatic method is reported for the synthesis of cis and trans P-amino acid enantiomers through the lipase-catalyzed enantioselective hydrolysis of alicyclic beta-amino esters in organic media. High enantioselectivities (E usually > 100) were observed when the Candida antarctica lipase B catalyzed reactions were performed with H2O (0.5 equivalents) in iPr(2)O at 65 degrees C. The resolved products, obtained in good yields (>= 42%), could be easily separated.},
	year = {2007},
	eissn = {1521-3765},
	pages = {6397-6401},
	orcid-numbers = {Forró, Enikő/0000-0001-6796-3889; 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}
}

@article{MTMT:3038970,
	title = {Continuous-flow high pressure hydrogenation reactor for optimization and high-throughput synthesis},
	url = {https://m2.mtmt.hu/api/publication/3038970},
	author = {Jones, Richard and Godorhazy, L and Varga, N and Szalay, D and Urge, L and Darvas, Ferenc},
	doi = {10.1021/cc050107o},
	journal-iso = {J COMB CHEM},
	journal = {JOURNAL OF COMBINATORIAL CHEMISTRY},
	volume = {8},
	unique-id = {3038970},
	issn = {1520-4766},
	abstract = {This paper reports on a novel continuous-flow hydrogenation reactor and its integration with a liquid handler to generate a fully automated high-throughput hydrogenation system for library synthesis. The reactor, named the H-Cube, combines endogenous hydrogen generation from the electrolysis of water with a continuous flow-through system. The system makes significant advances over current batch hydrogenation reactors in terms of safety, reaction validation efficiency, and rates of reaction. The hydrogenation process is described along with a detailed description of the device's main parts. The reduction of a series of functional groups, varying in difficulty up to 70 °C and 70 bar are also described. The paper concludes with the integration of the device into an automated liquid handler followed by the reduction of a nitro compound in a high throughput manner. The system is fully automated and can conduct 5 reactions in the time it takes to perform and workup one reaction manually on a standard batch reactor. © 2006 American Chemical Society.},
	keywords = {PRESSURE; HEAT; ARTICLE; methodology; CATALYSIS; HYDROGENATION; molecular structure; chemical structure; instrumentation; combinatorial chemistry; Equipment Design; Combinatorial Chemistry Techniques},
	year = {2006},
	eissn = {1520-4774},
	pages = {110-116}
}

@article{MTMT:1012935,
	title = {Secondary structure dependent self-assembly of beta-peptides into nanosized fibrils and membranes},
	url = {https://m2.mtmt.hu/api/publication/1012935},
	author = {Martinek, Tamás and Hetényi, Anasztázia and Fülöp, Lívia and Mándity, István and Tóth, Gábor and Dékány, Imre and Fülöp, Ferenc},
	doi = {10.1002/anie.200504158},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {45},
	unique-id = {1012935},
	issn = {1433-7851},
	keywords = {ASSOCIATION; BETA-PEPTIDES; NANOFIBERS; ACID OLIGOMERS; PROTEINOGENIC SIDE-CHAINS; FOLDAMERS; nanomaterials; TERTIARY STRUCTURE; peptide mimetics},
	year = {2006},
	eissn = {1521-3773},
	pages = {2396-2400},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Hetényi, Anasztázia/0000-0001-8080-6992; Fülöp, Lívia/0000-0002-8010-0129; Mándity, István/0000-0003-2865-6143; Tóth, Gábor/0000-0002-3604-4385; Dékány, Imre/0000-0001-5472-5355; 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:1012850,
	title = {Chain-length-dependent helical motifs and self-association of beta-peptides with constrained side chains},
	url = {https://m2.mtmt.hu/api/publication/1012850},
	author = {Hetényi, Anasztázia and Mándity, István and Martinek, Tamás and Tóth, Gábor and Fülöp, Ferenc},
	doi = {10.1021/ja0475095},
	journal-iso = {J AM CHEM SOC},
	journal = {JOURNAL OF THE AMERICAN CHEMICAL SOCIETY},
	volume = {127},
	unique-id = {1012850},
	issn = {0002-7863},
	abstract = {Homo-oligomers constructed by using trans-2-aminocyclohexanecarboxylic
		acid monomers without protecting groups were studied. Both ab initio
		theory and NMR measurements showed that the tetramer tends to adopt a
		10-helix motif, while the pentamer and hexamer form the known 14-helix.
		It was concluded that the conformationally constrained backbone is
		flexible enough to afford both 10-helical and 14-helical motifs, this
		observation in turn providing evidence of the true folding process.
		Self-association or the helical units was also detected, and the
		results of variable-temperature diffusion NMR measurements strongly
		suggested the presence of helical bundles in methanol solution.},
	keywords = {AMINO-ACIDS; SECONDARY STRUCTURE; CIRCULAR-DICHROISM; MICELLIZATION; AQUEOUS-SOLUTION; ACID OLIGOMERS; FOLDAMERS; Hydrophobic interactions; TERTIARY STRUCTURE},
	year = {2005},
	eissn = {1520-5126},
	pages = {547-553},
	orcid-numbers = {Hetényi, Anasztázia/0000-0001-8080-6992; Mándity, István/0000-0003-2865-6143; Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385; 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}
}

@article{MTMT:1013825,
	title = {cis-2-aminocyclopentanecarboxylic acid oligomers adopt a sheetlike structure: Switch from helix to nonpolar strand},
	url = {https://m2.mtmt.hu/api/publication/1013825},
	author = {Martinek, Tamás and Tóth, Gábor and Vass, Elemér and Hollósi, Miklós and Fülöp, Ferenc},
	doi = {10.1002/1521-3773(20020517)41:10<1718::AID-ANIE1718>3.0.CO;2-2},
	journal-iso = {ANGEW CHEM INT EDIT},
	journal = {ANGEWANDTE CHEMIE-INTERNATIONAL EDITION},
	volume = {41},
	unique-id = {1013825},
	issn = {1433-7851},
	keywords = {SECONDARY STRUCTURE; SIDE-CHAINS; SPECTROSCOPY; BETA-PEPTIDES; FOLDAMERS; CHIRALITY; amino acids; conformation analysis; NMR spectroscopy; TURNS},
	year = {2002},
	eissn = {1521-3773},
	pages = {1718-1721},
	orcid-numbers = {Martinek, Tamás/0000-0003-3168-8066; Tóth, Gábor/0000-0002-3604-4385; Vass, Elemér/0000-0001-8898-3846; Fülöp, Ferenc/0000-0003-1066-5287}
}