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001-es BibID:	BIBFORM116643
035-os BibID:	(cikkazonosító)464286 (Scopus)85167593174 (WoS)001055045200001
Első szerző:	Andrási Melinda (gyógyszerész)
Cím:	Comparative study on the deamidation of three recombinant human insulins using capillary electrophoresis / M. Andrasi, G. Vishwakarma, R. Szabo, C. Nagy, A. Gaspar
Dátum:	2023
ISSN:	0021-9673
Megjegyzések:	The applicability of capillary zone electrophoresis (CZE) for the separation of different recombinant human insulins and their deamidated isoforms was studied. The high resolving power of CZE is demonstrated by its ability to separate insulin isoforms differing only by 0.984 Da (different-fold deamidated forms) and even components having the exacts same mass but slightly different shapes (same-fold deamidated forms). From among the several insulins available, humulin, glargine and glulisine were selected for our study because their sequences and chemical parameters are quite similar, however, the small differences present in their amino acid sequences influence the deamidation processes. Using a background electrolyte with basic pH was favourable not only for the separation of the different types of insulin but also for the separation of deamidated protein forms even in a bare fused silica capillary. The LOD values ranged between 0.6 - 0.93 mg/L and 2.17 - 4.37 mg/L for UV and ESI-MS detection, respectively. At -20 - -80 ?C, the deamidation is minimal, but at temperatures above +5 ?C deamidation is accelerated. At +5 ?C only 1-fold deamidation forms could be observed for each insulin. Acidified samples incubated for 1-month at room temperature showed varying levels of deamidation: 1-fold, 1?2-fold and 1?2?3-fold forms for glargine, glulisine and humulin, respectively.
Tárgyszavak:	Természettudományok Kémiai tudományok magyar nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Insulins Deamidation Isoforms Capillary electrophoresis Mass spectrometry
Megjelenés:	Journal of Chromatography A. - 1706 (2023), p. 1-8. -
További szerzők:	Vishwakarma, G. Szabó Ruben (1998-) Nagy Cynthia (1994-) Gáspár Attila (1970-) (vegyész, kémikus)
Pályázati támogatás:	K 142134 Egyéb ÚNKP-22-2-I-DE-193 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM117884
035-os BibID:	(cikkazonosító)342162 (WoS)001147540500001 (Scopus)85181709291
Első szerző:	Nagy Cynthia (1994-)
Cím:	CZE-MS peptide mapping : To desalt or not to desalt? / Cynthia Nagy, Melinda Andrasi, Ruben Szabo, Attila Gaspar
Dátum:	2024
ISSN:	0003-2670
Megjegyzések:	Background: In "shotgun" approaches involving high-performance liquid chromatography or capillary zone electrophoresis (CZE), matrix removal prior to sample analysis is considered as an indispensable tool. Despite the fact that CZE offers a high tolerance towards salts, most publications reported on the use of desalting. There seems to be no clear consensus on the utilization of desalting in the CZE-MS community, most probably due to the absence of works addressing the comparison of desalted and non-desalted digests. Our aim was to fill this research gap using protein samples of varying complexity in different sample matrices. Results: First, standard protein digests were analyzed to build the knowledge on the effect of sample clean-up by solid-phase extraction (SPE) pipette tips and the possible stacking phenomena induced by different sample matrices. Desalting led to a somewhat altered peptide profile, the procedure affected mostly the hydrophilic peptides (although not to a devastating extent). Nevertheless, desalting samples allowed remarkable stacking efficiency owing to their low-conductivity sample background, enabling a so-called field-amplified sample stacking phenomenon. Non-desalted samples also produced a stacking event, the mechanism of which is based on transient-isotachophoresis due to the presence of high-mobility ions in the digestion buffer itself. Adding either extra ammonium ions or acetonitrile into the non-desalted digests enhanced the stacking efficiency. A complex sample (yeast cell lysate) was also analyzed with the optimal conditions, which yielded similar tendencies. Significance: Based on these results, we propose that sample clean-up in the bottom-up sample preparation process prior to CZE-MS analysis can be omitted. The preclusion of desalting can even enhance detection sensitivity, separation efficiency or sequence coverage.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Bottom-up proteomics Capillary zone electrophoresis Desalting Mass spectrometry Peptide mapping
Megjelenés:	Analytica Chimica Acta. - 1288 (2024), p. 1-9. -
További szerzők:	Andrási Melinda (1979-) (gyógyszerész) Szabó Ruben (1998-) Gáspár Attila (1970-) (vegyész, kémikus)
Pályázati támogatás:	K-142134 Egyéb ÚNKP-22-3-II Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM106977
035-os BibID:	(WoS)000807738200001 (Scopus)85125010762 (Cikkazonosító)311
Első szerző:	Nagy Cynthia (1994-)
Cím:	Microfluidic Immobilized Enzymatic Reactors for Proteomic Analyses-Recent Developments and Trends (2017-2021) / Cynthia Nagy, Ruben Szabo, Attila Gaspar
Dátum:	2022
ISSN:	2072-666X
Megjegyzések:	: Given the strong interdisciplinary nature of microfluidic immobilized enzyme reactor (?-IMER) technology, several branches of science contribute to its successful implementation. A combination of physical, chemical knowledge and engineering skills is often required. The development and application of ?-IMERs in the proteomic community are experiencing increasing importance due to their attractive features of enzyme reusability, shorter digestion times, the ability to handle minute volumes of sample and the prospect of on-line integration into analytical workflows. The aim of this review is to give an account of the current (2017-2021) trends regarding the preparation of microdevices, immobilization strategies, and IMER configurations. The different aspects of microfabrication (designs, fabrication technologies and detectors) and enzyme immobilization (empty and packed channels, and monolithic supports) are surveyed focusing on ?-IMERs developed for proteomic analysis. Based on the advantages and limitations of the published approaches and the different applications, a probable perspective is given.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Micromachines. - 13 : 2 (2022), p. 1-19. -
További szerzők:	Szabó Ruben (1998-) Gáspár Attila (1970-) (vegyész, kémikus)
Pályázati támogatás:	K127931 OTKA K142134 OTKA ÚNKP-21-3-II Egyéb
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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001-es BibID:	BIBFORM098615
035-os BibID:	(cikkazonosító)5902 (WoS)000706517100001 (Scopus)85116118060
Első szerző:	Nagy Cynthia (1994-)
Cím:	Development of an In-Line Enzyme Reactor Integrated into a Capillary Electrophoresis System / Nagy Cynthia, Szabo Ruben, Gaspar Attila
Dátum:	2021
ISSN:	1420-3049
Megjegyzések:	The goal of this paper was to develop an in-line immobilized enzyme reactor (IMER) integrated into a capillary electrophoresis platform. In our research, we created the IMER by adsorbing trypsin onto the inner surface of a capillary in a short section. Enzyme immobilization was possible due to the electrostatic attraction between the oppositely charged fused silica capillary surface and trypsin. The reactor was formed by simply injecting and removing trypsin solution from the capillary inlet (similar to 1-2 cms). We investigated the factors affecting the efficiency of the reactor. The main advantages of the proposed method are the fast, cheap, and easy formation of an IMER with in-line protein digestion capability. Human tear samples were used to test the efficiency of the digestion in the microreactor.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Molecules. - 26 : 19 (2021), p. 1-14. -
További szerzők:	Szabó Ruben (1998-) Gáspár Attila (1970-) (vegyész, kémikus)
Pályázati támogatás:	K127931 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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