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001-es BibID:	BIBFORM084562
035-os BibID:	(Scopus)84961282078 (WOS)000379133500002
Első szerző:	Bodnár Judit
Cím:	Enzymatic removal of N-glycans by PNGase F coated magnetic microparticles / Bodnar Judit, Szekrenyes Akos, Szigeti Marton, Jarvas Gabor, Krenkova Jana, Foret Frantisek, Guttman Andras
Dátum:	2016
ISSN:	0173-0835 1522-2683
Megjegyzések:	Investigation of protein glycosylation is an important area in biomarker discovery and biopharmaceutical research. Alterations in protein N-glycosylation can be an indication of changes in pathological conditions in the medical field or production parameters of biotherapeutics. Rapid development of these disciplines calls for fast, high-throughput, and reproducible methods to analyze protein N-glycosylation. Currently used methods require either long deglycosylation times or large excess of enzymes. In this paper, we report on the use of PNGase F immobilization onto the surface of magnetic microparticles and their use in rapid and efficient removal of N-glycans from glycoproteins. The use of immobilized PNGase F also allowed reusability of the enzyme-coated beads as the magnetic microparticles can be readily partitioned from the sample by a magnet after each deglycosylation reaction. The efficiency and activity of the PNGase F coated magnetic beads was compared with in-solution enzyme reactions using standard glycoproteins possessing the major N-glycan types of neutral, high mannose, and highly sialylated carbohydrates. The PNGase F coated magnetic beads offered comparable deglycosylation level to the conventional in-solution based method in 10-min reaction times for the model glycoproteins of immunoglobulin G (mostly neutral carbohydrates), ribonuclease B (high mannose type sugars), and fetuin (highly sialylated oligosaccharides) with the special features of easy removal of the enzyme from the reaction mixture and reusability.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Deglycosylation Enzyme immobilization Magnetic microparticles PNGase F
Megjelenés:	Electrophoresis. - 37 : 10 (2016), p. 1264-1269. -
További szerzők:	Szekrényes Ákos (1983-) (vegyészmérnök) Szigeti Márton (1986-) (környezetmérnök) Járvás Gábor (1982-) (vegyészmérnök) Krenkova, Jana Foret, František Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K116263 NKFIH
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM073661
Első szerző:	Borza Beáta (biomérnök)
Cím:	Glycosimilarity assessment of biotherapeutics 1 : quantitative comparison of the N-glycosylation of the innovator and a biosimilar version of etanercept / Borza Beata, Szigeti Marton, Szekrenyes Akos, Hajba Laszlo, Guttman Andras
Dátum:	2018
ISSN:	0731-7085
Megjegyzések:	The carbohydrate moieties on the polypeptide chains in most glycoprotein based biotherapeutics and their biosimilars play essential roles in such major mechanisms of actions as antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity, anti-inflammatory functions and serum clearance. In addition, alteration in glycosylation may influence the safety and efficacy of the product. Glycosylation, therefore, is considered as one of the important critical quality attributes of glycoprotein biotherapeutics, and consequently for their biosimilar counterparts. Thus, the carbohydrate moieties of such biopharmaceuticals (both innovator and biosimilar products) should be closely scrutinized during all stages of the manufacturing process. In this paper we introduce a rapid, capillary gel electrophoresis based process to quantitatively assess the glycosylation aspect of biosimilarity (referred to as glycosimilarity) between the innovator and a biosimilar version of etanercept (Enbrel? and Benepali?, respectively), based on their N-linked carbohydrate profiles. Differences in sialylated, core fucosylated, galactosylated and high mannose glycans were all quantified. Since the mechanism of action of etanercept is TNF? binding, only mannosylation was deemed as critical quality attribute for glycosimilarity assessment due to its influence on serum half-life.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Pharmaceutical and Biomedical Analysis. - 153 (2018), p. 182-185. -
További szerzők:	Szigeti Márton (1986-) (környezetmérnök) Szekrényes Ákos (1983-) (vegyészmérnök) Hajba László Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	K 116263 NKFIH GINOP-2.3.2-15-2016-00017 GINOP
Internet cím:	Szerző által megadott URL Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM083126
035-os BibID:	(WoS)000508387300020 (Scopus)85075579456
Első szerző:	Szekrényes Ákos (vegyészmérnök)
Cím:	Quantitative comparison of the N-glycosylation of therapeutic glycoproteins using the Glycosimilarity Index. A tutorial / Szekrenyes Akos, Szigeti Marton, Dvorakova Veronika, Jarvas Gabor, Guttman Andras
Dátum:	2020
ISSN:	0165-9936
Megjegyzések:	Glycosylation is considered as one of the crucial critical quality attributes of therapeutic glycoproteins and for their biosimilar counterparts. Carbohydrate moieties of such biopharmaceuticals should be closely monitored during all stages of development and manufacturing and studied accordingly during comparability or similarity exercises. In therapeutic glycoprotein production, the batch-to-batch alteration in glycosylation represents an excellent indicator of process robustness. Due to the complexity of the obtained glycoanalytical profile it is challenging to determine and describe the level of similarity between the N-glycosylation characteristics of two glycoprotein production lots or between the reference batch and its biosimilar versions. In this tutorial, we provide a step-by-step approach to calculate a numerical similarity value of N-glycosylation, referred to as Glycosimilarity Index that can be efficiently used to assess the conformity degree of any new N-glycosylation profile to a given target profile.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Trac-Trends In Analytical Chemistry. - 122 (2020), p. 1-8. -
További szerzők:	Szigeti Márton (1986-) (környezetmérnök) Dvorakova, Veronika Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	BIONANO_GINOP-2.3.2-15-2016-00017 GINOP K116263 NKFIH NN127062 NKFIH 2018-2.1.17-TET-KR-2018-00010 NKFIH
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM084744
Első szerző:	Szigeti Márton (környezetmérnök)
Cím:	Rapid N -glycan release from glycoproteins using immobilized PNGase F microcolumns / Szigeti Marton, Bondar Judit, Gjerde Douglas, Keresztessy Zsolt, Szekrenyes Akos, Guttman Andras
Dátum:	2016
ISSN:	1570-0232
Megjegyzések:	N-glycosylation profiling of glycoprotein biotherapeutics is an essential step in each phase of product development in the biopharmaceutical industry. For example, during clone selection, hundreds of clones should be analyzed quickly from limited amounts of samples. On the other hand, identification of disease related glycosylation alterations can serve as early indicators (glycobiomarkers) for various pathological conditions in the biomedical field. Therefore, there is a growing demand for rapid and easy to automate sample preparation methods for N-glycosylation analysis. In this paper, we report on the design and implementation of immobilized recombinant glutathione-S-transferase (GST) tagged PNGase F enzyme microcolumns for rapid and efficient removal of N-linked carbohydrates from glycoproteins. Digestion speed and efficiency were compared to conventional in-solution based protocols. The use of PNGase F functionalized microcolumns resulted in efficient N-glycan removal in 10 min from all major N-linked glycoprotein types of: (i) neutral (IgG), (ii) highly sialylated (fetuin), and (iii) high mannose (ribonuclease B) carbohydrate containing glycoprotein standards. The approach can be readily applied to automated sample preparation systems, such as liquid handling robots.
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk N-glycosylation Enzyme immobilization PNGase F Capillary electrophoresis
Megjelenés:	Journal Of Chromatography B-Analytical Technologies In The Biomedical And Life Sciences. - 1032 (2016), p. 139-143. -
További szerzők:	Bondar Judit Gjerde, Douglas Keresztessy Zsolt Szekrényes Ákos (1983-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:	NKFIH-K116263 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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