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1.

001-es BibID:BIBFORM106796
035-os BibID:(scopus)85130784505 (wos)000833521000006
Első szerző:Farsang Róbert
Cím:Immobilized exoglycosidase matrix mediated solid phase glycan sequencing / Farsang Róbert, Kovács Noémi, Szigeti Márton, Jankovics Hajnalka, Vonderviszt Ferenc, Guttman András
Dátum:2022
ISSN:0003-2670
Megjegyzések:Full characterization of the attached carbohydrate moieties of glycoproteins is of high importance for both the rapidly growing biopharmaceutical industry and the biomedical field. In this paper we report the design and production of three important 6HIS-tagged exoglycosidases (neuraminidase, ?-galactosidase and hexosaminidase) to support rapid solid phase N-glycan sequencing with high robustness using immobilized enzymes. The exoglycosidases were generated in bacterial expression systems with high yield. Oriented immobilization via the 6HIS-tag portion of the molecules supported easy accessibility to the active sites and consequently high digestion performance. The three exoglycosidases were premixed in an appropriate matrix format and processed in a low-salt buffer to support long term storage. The digestion efficiencies of the immobilized enzymes were demonstrated by using solid phase sequencing in conjunction with capillary electrophoresis analysis of the products on a commercial glycoprotein therapeutic (palivizumab) and human serum derived fluorophore labeled glycans.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytica Chimica Acta. - 1215 (2022), p. 1-8. -
További szerzők:Kovács Noémi Szigeti Márton (1986-) (környezetmérnök) Jankovics Hajnalka Vonderviszt Ferenc Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:BIONANO_GINOP-2.3.2-15-2016-00017
Egyéb
2020-4.1.1-TKP2020
Egyéb
NN 127062
Egyéb
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2.

001-es BibID:BIBFORM096236
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:Capillary sodium dodecyl sulfate gel electrophoresis of proteins : introducing the three dimensional Ferguson method / Csenge Filep, András Guttman
Dátum:2021
ISSN:0003-2670
Megjegyzések:One of the most extensively utilized rapid characterization, release and stability testing methods of therapeutic proteins in the biopharmaceutical field today is capillary SDS gel electrophoresis using borate cross-linked high molecular weight dextran. In spite of its widespread use, however, the gel composition dependent separation characteristics of this very unique sieving matrix has not been investigated yet. Introduction of three dimensional (3D) Ferguson plots, based on simultaneous variation of the dextran (D) and borate (B) concentrations generating 16 different D/B ratio gels, allowed better understanding of the electromigration process of the SDS-protein complexes. As a result of this comprehensive study, non-linear 3D logarithmic mobility vs dextran and borate concentration surfaces were obtained. Both, the molecular weight protein standards and the new modality fusion protein etanercept resulted in concave 3D Ferguson plots. The interplay between the electroosmotic flow and the viscosity of the matrices played a key role in the resulting migration time and resolution. Selectivity values were defined and evaluated in 3D graph formats for the regular and de-N-glycosylated subunits of etanercept, as well as for the latter with the 10 kDa internal standard to understand both the dextran-borate complexation and sized based selectivities. KR plots of the retardation coefficients as the function of the logarithmic molecular weights were used to more precisely assess the Mw of the samples and to obtain information about the molecular characteristics of the electromigrating SDS-protein complexes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytica Chimica Acta. - 1183 (2021), p. 1-9. -
További szerzők:Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:BIONANO
Egyéb
ÚNKP-20-3-II-DE-294
Egyéb
TKP2020-IKA-07
Egyéb
NKFIH
Egyéb
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3.

001-es BibID:BIBFORM095052
Első szerző:Filep Csenge Boróka (biomérnök)
Cím:Multilevel capillary gel electrophoresis characterization of new antibody modalities / Csenge Filep, Marton Szigeti, Robert Farsang, Markus Haberger, Dietmar Reusch, Andras Guttman
Dátum:2021
ISSN:0003-2670
Tárgyszavak:Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
New modalities
Monoclonal antibody
SDS-CGE
N-Glycan analysis
Trypsin digestion
Megjelenés:Analytica Chimica Acta. - 1166 (2021), p. 1-9. -
További szerzők:Szigeti Márton (1986-) (környezetmérnök) Farsang Róbert Haberger, Markus Reusch, Dietmar Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:2.3.2- 15-2016-00017
GINOP
2018-2.1.17-TÉT-KR-2018-00010
Egyéb
TKP2020-IKA-07
Egyéb
UNKP-20-5
Egyéb
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4.

001-es BibID:BIBFORM099695
Első szerző:Reider Balázs
Cím:Integrated workflow for urinary prostate specific antigen N-glycosylation analysis using sdAb partitioning and downstream capillary electrophoresis separation / Reider Balazs, Gacsi Eszter, Jankovics Hajnalka, Vonderviszt Ferenc, Szarvas Tibor, Guttman Andras, Jarvas Gabor
Dátum:2021
ISSN:0003-2670
Megjegyzések:Prostate cancer represents the second highest malignancy rate in men in all cancer diagnoses worldwide. The development and progression of prostate cancer is not completely understood yet at molecular level, but it has been reported that changes in the N-glycosylation of prostate-specific antigen (PSA) occur during tumor genesis. In this paper we report on the development and implementation of a highthroughput capillary electrophoresis based glycan analysis workflow for urinary PSA analysis. The technology utilizes selective, high yield single domain antibody based PSA capture, followed by preconcentration and capillary electrophoresis coupled with laser-induced fluorescence detection, resulting in high resolution N-glycan profiles. Urinary PSA glycan profiles were compared to a commercially available PSA standard revealing differences in their a2,3- and a2,6-sialylated isomers, proving the excellent selectivity of the suggested workflow. This is important as sialylation classification plays an important role in the differentiation between indolent, significant and aggressive forms of prostate cancer.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytica Chimica Acta. - 1184 (2021), p. 1-10. -
További szerzők:Gacsi Eszter Jankovics Hajnalka Vonderviszt Ferenc Szarvas Tibor (matematikus informatikus) Guttman András (1954-) (vegyészmérnök) Járvás Gábor (1982-) (vegyészmérnök)
Pályázati támogatás:2018e2.1.17- T ET-KR-2018-00010
Egyéb
UNKP-20-5
Egyéb
TKP2020-IKA-07
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM130039
035-os BibID:(scopus)105004261149 (wos)001490430400001
Első szerző:Sárközy Dániel (PhD hallgató)
Cím:Rapid baseline hump-free analysis of therapeutic proteins in a wide molecular weight range by SDS - capillary agarose gel electrophoresis / Sárközy Dániel, Farkas Anna, Guttman András
Dátum:2025
ISSN:0003-2670
Megjegyzések:Background: Sodium dodecyl sulfate capillary gel electrophoresis traditionally employs entangled polymer networks (CE-SDS) or borate cross-linked gels (SDS-CGE) for size-based protein analysis. However, the separation of SDS proteins in these transiently cross-linked sieving matrices requires long analysis times and in addition, baseline humps/waves frequently occur making peak identification and quantification challenging. The analytical biopharma community has been trying to solve this problem for a decade, making it clear that a novel gel composition was required to provide baseline hump-free separation of SDS-proteins by capillary electrophoresis of higher MW biopharmaceuticals. Results: Using a transiently cross-linked agarose matrix shown in this paper enabled rapid separation of therapeutic proteins with excellent resolution, but more importantly, eliminated the commonly observed baseline disturbances of dextran-based gel formulations. Using capillaries as short as 10 cm effective length, the tetrahydroxyborate cross-linked agarose matrix supported fast analysis (~5 min) of an intact anti-SARS-CoV-2 therapeutic antibody and its subunits with excellent run-to-run migration time (RSD <0.3 %) and peak area (RSD <5 %) reproducibility. High resolution between the closely migrating non-glycosylated heavy chain and the heavy chain fragments was also obtained (RS = 1.65). The high molecular weight thyroglobulin (660 kDa), and the highly glycosylated fusion protein of etanercept were also successfully analyzed with borate-agarosebased gels, exploiting the stable baseline at the upper molecular weight range of the separation trace.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Capillary gel electrophoresis
Agarose
Sodium dodecyl sulfate
Therapeutic proteins
Baseline hump
Megjelenés:Analytica Chimica Acta. - 1360 (2025), p. 1-5. -
További szerzők:Farkas Anna (1988-) (molekuláris biológus) Guttman András (1954-) (vegyészmérnök)
Pályázati támogatás:NKFIH ADVANCED 150780
Egyéb
DE Publikációs Tudománytámogatási Program
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6.

001-es BibID:BIBFORM092909
035-os BibID:(WoS)000579368600001 (Scopus)85089666849
Első szerző:Shao, Huikai
Cím:On-line enrichment of N-glycans by immobilized metal-affinity monolith for capillary electrophoresis analysis / Huikai Shao, Balazs Reider, Gabor Jarvas, Andras Guttman, Zhengjin Jiang, N. Thuy Tran, Myriam Taverna
Dátum:2020
ISSN:0003-2670
Megjegyzések:A novel N-glycan enrichment strategy is presented using unexpected but strong interactions between the sulfonate groups brought by the fluorescent dye of glycans and the Zr4+ modified poly(ethylene glycol methacrylate phosphate (EGMP)-co-acrylamide (AM)-co-bis-acrylamide (BAA)) monolith. The poly (EGMP-co-AM-co-BAA) monolith was synthesized via ultraviolet (UV) irradiation and then functionalized with Zr4+. The obtained monolith was characterized with scanning electron microscopy and mercury intrusion porosimetry. Large through-pores and a continuous skeleton with high permeability were observed. The N-glycans were labeled with the 1-aminopyrene-3, 6, 8-trisulfonic acid (APTS) and enriched by the Zr4+ modified monolith through IMAC interaction. This enrichment step was then coupled off-line to capillary electrophoresis (CE) separation with laser induced fluorescence (LIF) detection. Successful preconcentration of the APTS labeled maltooligosaccharide ladder was achieved under optimized conditions. Enrichment factors obtained for the maltooligosaccharides ranged from 9 to 24 with RSDs from 2.0% to 9.2% (n = 3). Moreover, very good repeatabilities (<6.7%) were obtained for glucose oligomers (4?15 glucose units) corresponding to sizes expected for N-glycans, demonstrating the great potential of this Zr4+ modified monolith to enrich APTS labeled glycans from N-glycoproteins. The proposed method was then successfully applied for the enrichment of N-glycans released from Ribonuclease B, in which case all five expected oligomannose glycans (Man 5 to Man 9) were successfully enriched. Thanks to the advantage of the method to enrich selectively APTS-glycans compared to the commercial SPE columns composed of HILIC or PGC materials, the first proof of concept of on-line enrichment coupled to CE-LIF separation was demonstrated for maltooligosaccharides as well.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytica Chimica Acta. - 1134 (2020), p. 1-9. -
További szerzők:Reider Balázs Járvás Gábor (1982-) (vegyészmérnök) Guttman András (1954-) (vegyészmérnök) Jiang, Zhengjin Tran, N. Thuy Taverna, Myriam
Pályázati támogatás:BIONANO_GINOP-2.3.2-15-2016-00017
GINOP
ÚNKP-19-4
egyéb
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7.

001-es BibID:BIBFORM106821
035-os BibID:(scopus)85128474989 (wos)000804191600005
Első szerző:Shrivastava, Anuj
Cím:N-Glycosylation of monoclonal antibody therapeutics : A comprehensive review on significance and characterization / Shrivastava Anuj, Joshi Srishti, Guttman Andras, Rathore Anurag S.
Dátum:2022
ISSN:0003-2670
Megjegyzések:N-glycosylation of therapeutic antibodies starts as a co-translational step followed by a set of post-translational modifications and is considered as one of the critical quality attributes because of its impact on biological functions as well as therapy outcome. In addition to detailed product characterization of these glycans by the manufacturers, their comprehensive analysis is also a regulatory requirement. However, the structural complexity and heterogeneity of these N-linked carbohydrates make their characterization quite challenging. In this review, we give a comprehensive overview of N-glycosylation diversity and its functional importance for monoclonal antibody therapeutic products. A descriptive coverage is also provided for the various strategies and techniques employed for oligosaccharide characterization, that include analysis of intact-glycoproteins, their sub-units, glycopeptides as well as released glycans through chromatographic, electrophoretic and spectroscopic techniques. To assist the readers, relevant examples from the literature are cited and critically discussed for each of the strategies and techniques. To conclude, a discussion on unique challenges associated with the analysis of this important post-translational modification is presented.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Analytica Chimica Acta. - 1209 (2022), p. 1-18. -
További szerzők:Joshi, Srishti Guttman András (1954-) (vegyészmérnök) Rathore, Anurag S.
Pályázati támogatás:2018-2.1.17-TÉT-KR-201800010
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