@article{MTMT:3054649,
	title = {Small Peptides Derived from Penetratin as Antibacterial Agents},
	url = {https://m2.mtmt.hu/api/publication/3054649},
	author = {Parravicini, Oscar and Somlai, Csaba and Andujar, Sebastian A and Garro, Adriana D and Lima, Beatriz and Tapia, Alejandro and Feresin, Gabriela and Perczel, András and Tóth, Gábor and Cascales, Javier Lopez and Rodriguez, Ana M and Enriz, Ricardo D},
	doi = {10.1002/ardp.201500419},
	journal-iso = {ARCH PHARM},
	journal = {ARCHIV DER PHARMAZIE},
	volume = {349},
	unique-id = {3054649},
	issn = {0365-6233},
	abstract = {The synthesis, in vitro evaluation and conformational study of several small-size peptides acting as antibacterial agents are reported. Among the compds. evaluated, the peptides Arg-Gln-Ile-Lys-Ile-Trp-Arg-Arg-Met-Lys-Trp-Lys-Lys-NH2, Arg-Gln-Ile-Lys-Ile-Arg-Arg-Met-Lys-Trp-Arg-NH2, and Arg-Gln-Ile-Trp-Trp-Trp-Trp-Gln-Arg-NH2 exhibited significant antibacterial activity. These were found to be very active antibacterial compds., considering their small mol. size. To better understand the antibacterial activity obtained for these peptides, an exhaustive conformational anal. was performed, using both theor. calcns. and exptl. measurements. Mol. dynamics simulations using two different media (water and trifluoroethanol/water) were employed. The results of these theor. calcns. were corroborated by exptl. CD measurements. A brief discussion on the possible mechanism of action of these peptides at mol. level is also presented. Some of the peptides reported here constitute very interesting structures to be used as starting compds. for the design of new small-size peptides possessing antibacterial activity. [on SciFinder(R)]},
	keywords = {penetratin deriv peptide antibacterial conformation},
	year = {2016},
	eissn = {1521-4184},
	pages = {242-251},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Tóth, Gábor/0000-0002-3604-4385}
}

@article{MTMT:2550508,
	title = {Unusual enantioselectivities in heterogeneous organocatalyzed reactions: Reversal of direction using proline di- versus tri-peptides in the aldol addition},
	url = {https://m2.mtmt.hu/api/publication/2550508},
	author = {Szőllősi, György and Csámpai, Antal and Somlai, Csaba and Fekete, M and Bartók, Mihály},
	doi = {10.1016/j.molcata.2013.11.011},
	journal-iso = {J MOL CATAL A-CHEM},
	journal = {JOURNAL OF MOLECULAR CATALYSIS A-CHEMICAL},
	volume = {382},
	unique-id = {2550508},
	issn = {1381-1169},
	keywords = {PEPTIDES; HETEROGENEOUS CATALYSIS; asymmetric synthesis; organocatalysis; aldol reaction},
	year = {2014},
	eissn = {1873-314X},
	pages = {86-92},
	orcid-numbers = {Szőllősi, György/0000-0003-4418-9530; Csámpai, Antal/0000-0003-2107-7309}
}

@article{MTMT:2386687,
	title = {Penetratin and derivatives acting as antibacterial agents},
	url = {https://m2.mtmt.hu/api/publication/2386687},
	author = {Garro, AD and Olivella, MS and Bombasaro, JA and Lima, B and Tapia, A and Feresin, G and Perczel, András and Somlai, Csaba and Penke, Botond and López, Cascales J and Rodríguez, AM and Enriz, RD},
	doi = {10.1111/cbdd.12143},
	journal-iso = {CHEM BIOL DRUG DES},
	journal = {CHEMICAL BIOLOGY & DRUG DESIGN},
	volume = {82},
	unique-id = {2386687},
	issn = {1747-0277},
	abstract = {The synthesis, in vitro evaluation and conformational study of penetratin and structurally related derivatives acting as antibacterial agents are reported. Among the compounds evaluated here, two methionine sulphoxide derivatives (RQIKIWFQNRRM[O]KWKK-NH2 and RQIKIFFQNRRM[O]KFKK-NH2) exhibited the strongest antibacterial effect in this series. In order to better understand the antimicrobial activity obtained for these peptides, we performed an exhaustive conformational analysis using different approaches. Molecular dynamics simulations were performed using two different media (water and trifluoroethanol/water). The results of these theoretical calculations were corroborated using experimental CD measurements. The electronic study for these peptides was carried out using molecular electrostatic potentials obtained from RHF/6-31G(d) calculations. In addition, the non-apeptide RQIRRWWQR-NH2 showed strong inhibitory action against the Gram-negative and Gram-positive bacteria tested in this study. In this study we report the synthesis, in vitro evaluation, and conformational study of penetratin and structurally related derivatives acting as antibacterial agents. Among the compounds evaluated two methionine sulfoxide derivatives (RQIKIWFQNRRM[O] KWKK-NH2 and RQIKIFFQNRRM[O]KFKK-NH2) and a nonapeptide (RQIRRWWQR-NH2) exhibited the strongest antibacterial effect against the Gram-negative and Gram-positive bacteria tested in this study.© 2013 John Wiley and Sons A/S.},
	keywords = {ARTICLE; amino acid substitution; priority journal; controlled study; nonhuman; in vitro study; Circular Dichroism; antiinfective agent; molecular dynamics; Conformational study; Small-size peptides; PENETRATIN; antibacterial activity; bacterial growth; structure activity relation; drug synthesis; Negibacteria; gram negative bacterium; Gram positive bacterium; Posibacteria; methionine sulfoxide; Methionine sulphoxide derivatives},
	year = {2013},
	eissn = {1747-0285},
	pages = {167-177},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:1993696,
	title = {Synthesis and cytotoxic activity of 4-N-carboxybutyl-5-fluorocytosyl-Arg-Gln-Trp-Arg-Arg-Trp-Trp-Gln-Arg-NH2},
	url = {https://m2.mtmt.hu/api/publication/1993696},
	author = {Somlai, Csaba and Correche, Estela and Olivella, Monica and Tolosa, Laia and Lechon, Maria Jose Gomez and Dombi, György and Tóth, Gábor and Penke, Botond and Enriz, Ricardo D},
	doi = {10.1016/j.bmcl.2012.05.045},
	journal-iso = {BIOORG MED CHEM LETT},
	journal = {BIOORGANIC & MEDICINAL CHEMISTRY LETTERS},
	volume = {22},
	unique-id = {1993696},
	issn = {0960-894X},
	abstract = {The chem. synthesis of 4-N-carboxybutyl-5-fluorocytosine in soln. phase starting from 5-fluorocytosine and the solid phase synthesis of Arg-Gln-Trp-Arg-Arg-Trp-Trp-Gln-Arg-NH2 attached to the 4-N-carboxybutyl-5-fluorocytosine residue at the N-terminus of the peptide via peptide bond formation is reported. The target compd. exhibited a significant cytotoxic activity against a culture of HepG2 cells. In addn. our results demonstrated that this new compd. affect cell viability, produce mitochondrial dysfunction as well as interfere with intracellular calcium homeostasis control; leading to cell malfunction and death. [on SciFinder(R)]},
	keywords = {peptide carboxybutyl fluorocytosyl synthesis cytotoxic activity antitumor},
	year = {2012},
	eissn = {1464-3405},
	pages = {4233-4237},
	orcid-numbers = {Tóth, Gábor/0000-0002-3604-4385; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:1845203,
	title = {Respiratory consequences of red sludge dust inhalation in rats},
	url = {https://m2.mtmt.hu/api/publication/1845203},
	author = {Czövek, Dorottya and Novák, Zoltán and Somlai, Csaba and Asztalos, T and Tiszlavicz, László and Bozóki, Zoltán and Ajtai, Tibor and Utry, Noémi and Filep, Ágnes and Bari, Ferenc and Peták, Ferenc},
	doi = {10.1016/j.toxlet.2011.12.006},
	journal-iso = {TOXICOL LETT},
	journal = {TOXICOLOGY LETTERS},
	volume = {209},
	unique-id = {1845203},
	issn = {0378-4274},
	abstract = {The environmental disaster following flooding by red sludge in the Ajka region in Hungary poses a serious public health threat with particular concern regarding the potentially adverse respiratory effects of the inhalation of red sludge dust (RSD). The respiratory consequences of the inhalation of RSD obtained from field samples were investigated in rats. Rats were either exposed to RSD at a high concentration (2 weeks, 8h/day), or kept in room air. After the exposures, the airway resistance (R(aw)) and the respiratory tissues mechanics were measured under baseline condition, and following methacholine (MCh) challenges with the aim of establishing airway hyper-responsiveness (AH). Histopathology was performed to assess lung morphologic alterations. The physical properties and the chemical composition of the RSD were also characterized. The size distribution, chemical composition and topology of the RSD particles applied in our experiments were similar to those observed at the site of the disaster. The inhalation of RSD did not alter the basal respiratory mechanics, whereas it led to greater MCh-induced responses in R(aw), demonstrating the progression of mild AH. Histopathological investigations revealed fine, granular particles in the alveolar macrophages, as evidence that RSD had reached the lower respiratory tract and induced mild inflammation around the alveoli and the pulmonary vasculature. The mild respiratory symptoms that developed following short-term exposure of healthy individuals to high concentrations of airborne RSD do not appear to pose a greater respiratory hazard than the inhalation of urban dust at a comparable concentration.},
	year = {2012},
	eissn = {1879-3169},
	pages = {113-120},
	orcid-numbers = {Czövek, Dorottya/0000-0002-6542-5849; Tiszlavicz, László/0000-0003-1134-6587; Peták, Ferenc/0000-0001-6249-9327}
}

@article{MTMT:1880324,
	title = {Heat-shock protein 90 inhibition in autoimmunity to type VII collagen: evidence that nonmalignant plasma cells are not therapeutic targets},
	url = {https://m2.mtmt.hu/api/publication/1880324},
	author = {Kasperkiewicz, M and Muller, R and Manz, R and Magens, M and Hammers, CM and Somlai, Csaba and Westermann, J and Schmidt, E and Zillikens, D and Ludwig, RJ and Orosz, Antal},
	doi = {10.1182/blood-2010-10-314609},
	journal-iso = {BLOOD},
	journal = {BLOOD},
	volume = {117},
	unique-id = {1880324},
	issn = {0006-4971},
	abstract = {Blocking heat-shock protein 90 (Hsp90) induces death of malignant plasma cells by activation of the unfolded protein response, a signaling pathway activated by accumulation of misfolded proteins within the endoplasmic reticulum. We hypothesized that nontransformed plasma cells are also hypersensitive to Hsp90 inhibition because of their high amount of protein biosynthesis. To investigate this hypothesis, 2 different Hsp90 inhibitors, the geldanamycin derivative 17-DMAG and the nontoxic peptide derivative TCBL-145, were applied to mice with experimental epidermolysis bullosa acquisita, an autoimmune bullous disease characterized by autoantibodies against type VII collagen of the dermal-epidermal junction. Both inhibitors ameliorated clinical disease of type VII collagen-immunized mice, suppressed auto-antibody production, and reduced dermal neutrophilic infiltrate. Interestingly, total plasma cell numbers, type VII collagen-specific plasma cells, and germinal center B cells were unaffected by anti-Hsp90 treatment in vivo. However, T-cell proliferation was potently inhibited, as evidenced by the reduced response of isolated lymph node cells from immunized mice to in vitro restimulation with anti-CD3/CD28 antibody or autoantigen in the presence of Hsp90 inhibitors. Our results suggest that Hsp90 blockade has no impact on normal or autoreactive plasma cells in vivo and indentify T cells as targets of anti-Hsp90 treatment in autoimmunity to type VII collagen. (Blood. 2011;117(23):6135-6142)},
	keywords = {DISEASE; IDENTIFICATION; MICE; AUTOANTIBODIES; T-CELLS; ANTIBODIES; IMMUNOGLOBULIN; Toll-Like Receptors; bortezomib; EPIDERMOLYSIS-BULLOSA-ACQUISITA},
	year = {2011},
	eissn = {1528-0020},
	pages = {6135-6142}
}

@article{MTMT:1880323,
	title = {Heat shock protein 90 inhibition in autoimmunity to type VII collagen},
	url = {https://m2.mtmt.hu/api/publication/1880323},
	author = {Kasperkiewicz, M and Muller, R and Manz, R and Magens, M and Hammers, C and Somlai, Csaba and Westermann, J and Schmidt, E and Zillikens, D and Ludwig, R and Orosz, Antal},
	journal-iso = {J INVEST DERMATOL},
	journal = {JOURNAL OF INVESTIGATIVE DERMATOLOGY},
	volume = {131},
	unique-id = {1880323},
	issn = {0022-202X},
	year = {2011},
	eissn = {1523-1747},
	pages = {S6-S6}
}

@article{MTMT:1876499,
	title = {Synthesis and Comparison of the Antitumor Activities of Steroids on ABCB1-transfected Mouse Lymphoma and Human Ovary Carcinoma},
	url = {https://m2.mtmt.hu/api/publication/1876499},
	author = {Serly, Julianna and Vincze, Irén and Somlai, Csaba and Hodoniczki, László and Molnár, József},
	doi = {10.2174/157018011794183833},
	journal-iso = {LETT DRUG DES DISCOV},
	journal = {LETTERS IN DRUG DESIGN AND DISCOVERY},
	volume = {8},
	unique-id = {1876499},
	issn = {1570-1808},
	year = {2011},
	eissn = {1875-628X},
	pages = {138-147}
}

@article{MTMT:1842710,
	title = {Penetratin analogues acting as antifungal agents},
	url = {https://m2.mtmt.hu/api/publication/1842710},
	author = {Garibotto, FM and Garro, AD and Rodriguez, AM and Raimondi, M and Zacchino, SA and Perczel, András and Somlai, Csaba and Penke, Botond and Enriz, RD},
	doi = {10.1016/j.ejmech.2010.10.025},
	journal-iso = {EUR J MED CHEM},
	journal = {EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY},
	volume = {46},
	unique-id = {1842710},
	issn = {0223-5234},
	abstract = {The synthesis, in vitro evaluation, and conformational study of penetratin analogues acting as antifungal agents are reported. Different peptides structurally related with penetratin were evaluated. Analogues of penetratin rich in Arg, Lys and Trp amino acids were tested. In addition, HFRWRQIKIWFQNRRM[O]KWKK-NH(2), a synthetic 20 amino acid peptide was also evaluated. These penetratin analogues displayed antifungal activity against human pathogenic strains including Candida albicans and Cryptococcus neoformans. In contrast, Tat peptide, a well-known cell penetrating peptide, did not show a significant antifungal activity against fungus tested here. We also performed a conformational study by means experimental and theoretical approaches (CD spectroscopic measurements and MD simulations). The electronic structure analysis was carried out from Molecular Electrostatic Potentials (MEP) obtained by using RHF/6-31G ab initio calculations. Our experimental and theoretical results permitted us to identify a topographical template which may provide a guide for the design of new peptides with antifungal effects. (C) 2010 Elsevier Masson SAS. All rights reserved.},
	keywords = {PEPTIDES; PANCREATIC TRYPSIN-INHIBITOR; CONFORMATIONAL-ANALYSIS; MOLECULAR-DYNAMICS; MULTIPLE-MINIMA PROBLEM; 3RD HELIX; ANTENNAPEDIA HOMEODOMAIN; ANTIMICROBIAL PEPTIDES; EMPIRICAL SOLVATION MODELS; Molecular electrostatic potentials; Conformational study; DRIVEN MONTE-CARLO; Candida albicans; HIV-1 TAT PROTEIN; Cryptococcus neoformans; Antifungals},
	year = {2011},
	eissn = {1768-3254},
	pages = {370-377},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Penke, Botond/0000-0003-0938-0567}
}

@article{MTMT:1842707,
	title = {New Small-Size Antifungal Peptides: Design, Synthesis and Antifungal Activity},
	url = {https://m2.mtmt.hu/api/publication/1842707},
	author = {Garro, AD and Garibotto, FM and Rodriguez, AM and Raimondi, M and Zacchino, SA and Perczel, András and Somlai, Csaba and Penke, Botond and Enriz, RD},
	doi = {10.2174/157018011795906785},
	journal-iso = {LETT DRUG DES DISCOV},
	journal = {LETTERS IN DRUG DESIGN AND DISCOVERY},
	volume = {8},
	unique-id = {1842707},
	issn = {1570-1808},
	abstract = {The synthesis, in vitro evaluation and conformational study of small-size peptides acting as antifungal agents are reported. These peptides displayed antifungal activity against human pathogenic strains including Candida albicans and Cryptococcus neoformans. Among the peptides reported here, RQWRRWWQR-NH(2) exhibited the strongest activity against Cryptococcus neoformans. Our results allowed us to reduce in size these bioactive peptides from 16 to 11 and to 9 amino acid residues in total. Despite their reduction, they still maintained and even enhanced the antifungal activity detected for penetratin. A conformational and electronic structure analysis on these peptides was also performed by using molecular mechanics calculations in conjunction with Molecular Electrostatic Potentials (MEP) maps.},
	keywords = {PEPTIDES; ANALOGS; PANCREATIC TRYPSIN-INHIBITOR; CONFORMATIONAL-ANALYSIS; POLYPEPTIDES; 3RD HELIX; ANTENNAPEDIA HOMEODOMAIN; EMPIRICAL SOLVATION MODELS; Molecular electrostatic potentials; DRIVEN MONTE-CARLO; Conformational and Electronic Study; Antifungals},
	year = {2011},
	eissn = {1875-628X},
	pages = {562-567},
	orcid-numbers = {Perczel, András/0000-0003-1252-6416; Penke, Botond/0000-0003-0938-0567}
}