@article{MTMT:34082424,
	title = {Optimizing the enzymatic release of MMAE from isoDGR-based small molecule drug conjugate by incorporation of a GPLG-PABC enzymatically cleavable linker},
	url = {https://m2.mtmt.hu/api/publication/34082424},
	author = {Zambra, Marco and Randelovic, Ivan and Talarico, Francesco and Borbély, Adina Noémi and Svajda, Laura and Tóvári, József and Mező, Gábor and Bodero, Lizeth and Colombo, Sveva and Arrigoni, Federico and Fasola, Elettra and Gazzola, Silvia and Piarulli, Umberto},
	doi = {10.3389/fphar.2023.1215694},
	journal-iso = {FRONT PHARMACOL},
	journal = {FRONTIERS IN PHARMACOLOGY},
	volume = {14},
	unique-id = {34082424},
	abstract = {Antibody-Drug Conjugates (ADCs) and Small Molecule-Drug Conjugates (SMDCs) represent successful examples of targeted drug-delivery technologies for overcoming unwanted side effects of conventional chemotherapy in cancer treatment. In both strategies, a cytotoxic payload is connected to the tumor homing moiety through a linker that releases the drug inside or in proximity of the tumor cell, and that represents a key component for the final therapeutic effect of the conjugate. Here, we show that the replacement of the Val-Ala- p -aminobenzyloxycarbamate linker with the Gly-Pro-Leu-Gly- p -aminobenzyloxycarbamate (GPLG-PABC) sequence as enzymatically cleavable linker in the SMDC bearing the cyclo [DKP -iso DGR] α V β 3 integrin ligand as tumor homing moiety and the monomethyl auristatin E (MMAE) as cytotoxic payload led to a 4-fold more potent anti-tumoral effect of the final conjugate on different cancer cell lines. In addition, the synthesized conjugate resulted to be significantly more potent than the free MMAE when tested following the “kiss-and-run” protocol, and the relative potency were clearly consistent with the expression of the α V β 3 integrin receptor in the considered cancer cell lines. In vitro enzymatic cleavage tests showed that the GPLG-PABC linker is cleaved by lysosomal enzymes, and that the released drug is observable already after 15 min of incubation. Although additional data are needed to fully characterize the releasing capacity of GPLG-PABC linker, our findings are of therapeutic significance since we are introducing an alternative to other well-established enzymatically sensitive peptide sequences that might be used in the future for generating more efficient and less toxic drug delivery systems.},
	year = {2023},
	eissn = {1663-9812},
	orcid-numbers = {Randelovic, Ivan/0000-0003-0161-0022; Borbély, Adina Noémi/0000-0002-5506-6555; Tóvári, József/0000-0002-5543-3204; Mező, Gábor/0000-0002-7618-7954}
}

@article{MTMT:33715979,
	title = {A Novel Fusion Protein System for the Production of Nanobodies and the SARS-CoV-2 Spike RBD in a Bacterial System},
	url = {https://m2.mtmt.hu/api/publication/33715979},
	author = {Nagy-Fazekas, Dóra and Stráner, Pál and Ecsédi, Péter and Taricska, Nóra and Borbély, Adina Noémi and Nyitray, László and Perczel, András},
	doi = {10.3390/bioengineering10030389},
	journal-iso = {BIOENGINEERING-BASEL},
	journal = {BIOENGINEERING},
	volume = {10},
	unique-id = {33715979},
	abstract = {Antibodies are key proteins of the immune system, and they are widely used for both research and theragnostic applications. Among them, camelid immunoglobulins (IgG) differ from the canonical human IgG molecules, as their light chains are completely missing; thus, they have only variable domains on their heavy chains (VHHs). A single VHH domain, often called a nanobody, has favorable structural, biophysical, and functional features compared to canonical antibodies. Therefore, robust and efficient production protocols relying on recombinant technologies are in high demand. Here, by utilizing ecotin, an Escherichia coli protein, as a fusion partner, we present a bacterial expression system that allows an easy, fast, and cost-effective way to prepare nanobodies. Ecotin was used here as a periplasmic translocator and a passive refolding chaperone, which allowed us to reach high-yield production of nanobodies. We also present a new, easily applicable prokaryotic expression and purification method of the receptor-binding domain (RBD) of the SARS-CoV-2 S protein for interaction assays. We demonstrate using ECD spectroscopy that the bacterially produced RBD is well-folded. The bacterially produced nanobody was shown to bind strongly to the recombinant RBD, with a Kd of 10 nM. The simple methods presented here could facilitate rapid interaction measurements in the event of the appearance of additional SARS-CoV-2 variants.},
	year = {2023},
	eissn = {2306-5354},
	orcid-numbers = {Stráner, Pál/0000-0003-2240-8501; Ecsédi, Péter/0000-0002-4700-125X; Taricska, Nóra/0000-0002-9721-953X; Borbély, Adina Noémi/0000-0002-5506-6555; Nyitray, László/0000-0003-4717-5994; Perczel, András/0000-0003-1252-6416}
}

@article{MTMT:33631672,
	title = {SREKA-targeted liposomes for highly metastatic breast cancer therapy},
	url = {https://m2.mtmt.hu/api/publication/33631672},
	author = {Vári, Balázs and Dókus, Endre Levente and Borbély, Adina Noémi and Gaál, Anikó and Mező, Diána and Randelovic, Ivan and Sólyom-Tisza, Anna and Varga, Zoltán and Szoboszlai, Norbert and Mező, Gábor and Tóvári, József},
	doi = {10.1080/10717544.2023.2174210},
	journal-iso = {DRUG DELIV},
	journal = {DRUG DELIVERY : JOURNAL OF DELIVERY AND TARGETING OF THERAPEUTIC AGENTS},
	volume = {30},
	unique-id = {33631672},
	issn = {1071-7544},
	keywords = {tumor metastasis; Targeted cancer therapy; Nanocarriers; SREKA peptide},
	year = {2023},
	eissn = {1521-0464},
	orcid-numbers = {Vári, Balázs/0000-0001-9919-1502; Dókus, Endre Levente/0000-0002-3472-9911; Borbély, Adina Noémi/0000-0002-5506-6555; Gaál, Anikó/0000-0003-4064-1825; Randelovic, Ivan/0000-0003-0161-0022; Varga, Zoltán/0000-0002-5741-2669; Szoboszlai, Norbert/0000-0002-3991-3996; Mező, Gábor/0000-0002-7618-7954; Tóvári, József/0000-0002-5543-3204}
}

@article{MTMT:33631637,
	title = {Targeting the Gastrin-Releasing Peptide Receptor (GRP-R) in Cancer Therapy: Development of Bombesin-Based Peptide–Drug Conjugates. Development of Bombesin-Based Peptide-Drug Conjugates.},
	url = {https://m2.mtmt.hu/api/publication/33631637},
	author = {Gomena, Jacopo and Vári, Balázs and Szabó, Rita (Oláhné) and Biri-Kovács, Beáta and Bősze, Szilvia and Borbély, Adina Noémi and Soós, Ádám and Randelovic, Ivan and Tóvári, József and Mező, Gábor},
	doi = {10.3390/ijms24043400},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {24},
	unique-id = {33631637},
	issn = {1661-6596},
	abstract = {Targeted tumour therapy has proved to be an efficient alternative to overcome the limitations of conventional chemotherapy. Among several receptors upregulated in cancer cells, the gastrin-releasing peptide receptor (GRP-R) has recently emerged as a promising target for cancer imaging, diagnosing and treatment due to its overexpression on cancerous tissues such as breast, prostate, pancreatic and small-cell lung cancer. Herein, we report on the in vitro and in vivo selective delivery of the cytotoxic drug daunorubicin to prostate and breast cancer, by targeting GRP-R. Exploiting many bombesin analogues as homing peptides, including a newly developed peptide, we produced eleven daunorubicin-containing peptide–drug conjugates (PDCs), acting as drug delivery systems to safely reach the tumour environment. Two of our bioconjugates revealed remarkable anti-proliferative activity, an efficient uptake by all three tested human breast and prostate cancer cell lines, high stability in plasma and a prompt release of the drug-containing metabolite by lysosomal enzymes. Moreover, they revealed a safe profile and a consistent reduction of the tumour volume in vivo. In conclusion, we highlight the importance of GRP-R binding PDCs in targeted cancer therapy, with the possibility of further tailoring and optimisation.},
	year = {2023},
	eissn = {1422-0067},
	orcid-numbers = {Gomena, Jacopo/0000-0001-6830-0796; Vári, Balázs/0000-0001-9919-1502; Biri-Kovács, Beáta/0000-0001-5803-9969; Borbély, Adina Noémi/0000-0002-5506-6555; Randelovic, Ivan/0000-0003-0161-0022; Tóvári, József/0000-0002-5543-3204; Mező, Gábor/0000-0002-7618-7954}
}

@misc{MTMT:33718828,
	title = {PEGylated liposomes in targeted cancer therapy using SREKA as targeting moiety},
	url = {https://m2.mtmt.hu/api/publication/33718828},
	author = {Vári, Balázs and Dókus, Endre Levente and Borbély, Adina Noémi and Gaál, Anikó and Mező, Diána and Randelovic, Ivan and Szoboszlai, Norbert and Mező, Gábor and Tóvári, József},
	unique-id = {33718828},
	year = {2022},
	orcid-numbers = {Vári, Balázs/0000-0001-9919-1502; Dókus, Endre Levente/0000-0002-3472-9911; Borbély, Adina Noémi/0000-0002-5506-6555; Gaál, Anikó/0000-0003-4064-1825; Randelovic, Ivan/0000-0003-0161-0022; Szoboszlai, Norbert/0000-0002-3991-3996; Mező, Gábor/0000-0002-7618-7954; Tóvári, József/0000-0002-5543-3204}
}

@article{MTMT:32782717,
	title = {Synthesis and Antiproliferative Activity of Novel Imipridone–Ferrocene Hybrids with Triazole and Alkyne Linkers},
	url = {https://m2.mtmt.hu/api/publication/32782717},
	author = {Czuczi, Tamás and Murányi, József and Bárány, Péter Tibor and Móra , István András and Borbély, Adina Noémi and Csala, Miklós and Csámpai, Antal},
	doi = {10.3390/ph15040468},
	journal-iso = {PHARMACEUTICALS-BASE},
	journal = {PHARMACEUTICALS},
	volume = {15},
	unique-id = {32782717},
	year = {2022},
	eissn = {1424-8247},
	orcid-numbers = {Borbély, Adina Noémi/0000-0002-5506-6555; Csala, Miklós/0000-0002-3829-4361; Csámpai, Antal/0000-0003-2107-7309}
}

@article{MTMT:32288001,
	title = {Altered Glycosylation of Human Alpha-1-Acid Glycoprotein as a Biomarker for Malignant Melanoma},
	url = {https://m2.mtmt.hu/api/publication/32288001},
	author = {Virág, Dávid and Kremmer, Tibor and Lőrincz, Kende Kálmán and Kiss, Norbert and Jobbágy, Antal and Bozsányi, Szabolcs and Gulyás, Lili and Wikonkál, Norbert and Schlosser, Gitta (Vácziné) and Borbély, Adina Noémi and Huba, Zsófia and Dalmadiné Kiss, Borbála and Antal, István and Ludányi, Krisztina},
	doi = {10.3390/molecules26196003},
	journal-iso = {MOLECULES},
	journal = {MOLECULES},
	volume = {26},
	unique-id = {32288001},
	issn = {1420-3049},
	year = {2021},
	eissn = {1420-3049},
	orcid-numbers = {Virág, Dávid/0000-0001-8411-0773; Lőrincz, Kende Kálmán/0000-0002-1861-1008; Kiss, Norbert/0000-0002-9947-1755; Jobbágy, Antal/0000-0001-8098-5302; Gulyás, Lili/0000-0002-8049-0921; Wikonkál, Norbert/0000-0003-4949-8711; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Borbély, Adina Noémi/0000-0002-5506-6555; Dalmadiné Kiss, Borbála/0000-0002-5774-7880; Antal, István/0000-0002-5434-201X; Ludányi, Krisztina/0000-0002-2380-9529}
}

@article{MTMT:31855083,
	title = {Structural Characterization of Daunomycin-Peptide Conjugates by Various Tandem Mass Spectrometric Techniques},
	url = {https://m2.mtmt.hu/api/publication/31855083},
	author = {Borbély, Adina Noémi and Pethő, Lilla and Szabó, Ildikó and Almajidi, Mohammed and Steckel, Arnold and Nagy, Tibor and Kéki, Sándor and Kalló, Gergő and Csősz, Éva and Mező, Gábor and Schlosser, Gitta (Vácziné)},
	doi = {10.3390/ijms22041648},
	journal-iso = {INT J MOL SCI},
	journal = {INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES},
	volume = {22},
	unique-id = {31855083},
	issn = {1661-6596},
	year = {2021},
	eissn = {1422-0067},
	orcid-numbers = {Borbély, Adina Noémi/0000-0002-5506-6555; Pethő, Lilla/0000-0002-0298-3341; Szabó, Ildikó/0000-0002-9844-7841; Almajidi, Mohammed/0000-0001-5153-8247; Steckel, Arnold/0000-0002-4423-0399; Nagy, Tibor/0000-0001-8568-914X; Kéki, Sándor/0000-0002-5274-6117; Csősz, Éva/0000-0003-4373-2175; Mező, Gábor/0000-0002-7618-7954; Schlosser, Gitta (Vácziné)/0000-0002-7637-7133}
}

@{MTMT:31917020,
	title = {Tandem mass spectrometry of daunorubicin-containing peptide conjugates},
	url = {https://m2.mtmt.hu/api/publication/31917020},
	author = {Schlosser, Gitta (Vácziné) and Al-Majidi, M. and Borbély, Adina Noémi and Pethő, Lilla and Szabó, Dániel and Dókus, Endre Levente and Mező, Gábor},
	booktitle = {Development of bioconjugates and their module constructs for targeted therapy of cancers with high mortality},
	unique-id = {31917020},
	year = {2020},
	pages = {55-59},
	orcid-numbers = {Schlosser, Gitta (Vácziné)/0000-0002-7637-7133; Borbély, Adina Noémi/0000-0002-5506-6555; Pethő, Lilla/0000-0002-0298-3341; Szabó, Dániel/0000-0003-3375-395X; Dókus, Endre Levente/0000-0002-3472-9911; Mező, Gábor/0000-0002-7618-7954}
}

@article{MTMT:31856717,
	title = {Linker Hydrophilicity Modulates the Anticancer Activity of RGD–Cryptophycin Conjugates},
	url = {https://m2.mtmt.hu/api/publication/31856717},
	author = {Anselmi, Michele and Borbély, Adina Noémi and Figueras, Eduard and Michalek, Carmela and Kemker, Isabell and Gentilucci, Luca and Sewald, Norbert},
	doi = {10.1002/chem.202003471},
	journal-iso = {CHEM-EUR J},
	journal = {CHEMISTRY-A EUROPEAN JOURNAL},
	volume = {27},
	unique-id = {31856717},
	issn = {0947-6539},
	year = {2020},
	eissn = {1521-3765},
	pages = {1015-1022},
	orcid-numbers = {Anselmi, Michele/0000-0001-6700-6456; Borbély, Adina Noémi/0000-0002-5506-6555; Figueras, Eduard/0000-0002-1853-9974; Kemker, Isabell/0000-0001-5430-2803; Gentilucci, Luca/0000-0001-9134-3161; Sewald, Norbert/0000-0002-0309-2655}
}