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Article ; Online: In situ

Mildner, Malte / Hanio, Simon / Endres, Sebastian / Scheller, Lena / Engel, Bettina / Castañar, Laura / Meinel, Lorenz / Pöppler, Ann-Christin

Analytical methods : advancing methods and applications

2024 Volume 16, Issue 10, Page(s) 1468–1472

Abstract: There are various commercially available setups for studying drug permeation, which differ in cost and manual labor. We explore an artificial membrane in an NMR tube to assess drug permeation with automated measurements. NMR-based concentrations were ... ...

Abstract	There are various commercially available setups for studying drug permeation, which differ in cost and manual labor. We explore an artificial membrane in an NMR tube to assess drug permeation with automated measurements. NMR-based concentrations were validated with HPLC and compared to a conventional setup. Setup-specific challenges and workarounds as well as future setup-designs for this and other applications are discussed.
MeSH term(s)	Magnetic Resonance Spectroscopy ; Membranes, Artificial ; Chromatography, High Pressure Liquid
Chemical Substances	Membranes, Artificial
Language	English
Publishing date	2024-03-07
Publishing country	England
Document type	Journal Article
ZDB-ID	2515210-5
ISSN	1759-9679 ; 1759-9660
ISSN (online)	1759-9679
ISSN	1759-9660
DOI	10.1039/d3ay01995k
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Article ; Online: Solid microemulsion preconcentrates on pH responsive metal-organic framework for tableting.

Scheller, Lena / Bachmann, Stephanie / Zorn, Theresa / Hanio, Simon / Gbureck, Uwe / Fatouros, Dimitrios / Pöppler, Ann-Christin / Meinel, Lorenz

European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V

2023 Volume 186, Page(s) 105–111

Abstract: Poorly water-soluble drugs are frequently formulated with lipid-based formulations including microemulsions and their preconcentrates. We detailed the solidification of drug-loaded microemulsion preconcentrates with the acid-sensitive metal-organic ... ...

Abstract	Poorly water-soluble drugs are frequently formulated with lipid-based formulations including microemulsions and their preconcentrates. We detailed the solidification of drug-loaded microemulsion preconcentrates with the acid-sensitive metal-organic framework ZIF-8 by X-ray powder diffraction and solid-state nuclear magnetic resonance spectroscopy. Adsorption and desorption dynamics were analyzed by fluorescence measurement, high-performance liquid chromatography, dynamic light scattering and
MeSH term(s)	Metal-Organic Frameworks ; Drug Delivery Systems ; Water/chemistry ; Emulsions/chemistry ; Lipids/chemistry ; Tablets ; Hydrogen-Ion Concentration
Chemical Substances	Metal-Organic Frameworks ; Water (059QF0KO0R) ; Emulsions ; Lipids ; Tablets
Language	English
Publishing date	2023-03-22
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1065368-5
ISSN	1873-3441 ; 0939-6411
ISSN (online)	1873-3441
ISSN	0939-6411
DOI	10.1016/j.ejpb.2023.03.010
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Article: A comparative study of CE‐SDS, SDS‐PAGE, and Simple Western—Precision, repeatability, and apparent molecular mass shifts by glycosylation

Scheller, Christin / Krebs, Finja / Wiesner, Rebecca / Wätzig, Hermann / Oltmann‐Norden, Imke

Electrophoresis. 2021 Aug., v. 42, no. 14-15

2021

Abstract: SDS gel electrophoresis is a commonly used approach for monitoring purity and apparent molecular mass (Mr) of proteins, especially in the field of quality control of biopharmaceutical proteins. The technological installation of CE‐SDS as the replacement ... ...

Abstract	SDS gel electrophoresis is a commonly used approach for monitoring purity and apparent molecular mass (Mr) of proteins, especially in the field of quality control of biopharmaceutical proteins. The technological installation of CE‐SDS as the replacement of the slab gel technique (SDS‐PAGE) is still in progress, leading to a continuous improvement of CE‐SDS instruments. Various CE‐SDS instruments, namely Maurice (CE‐SDS/CE‐SDS PLUS) and Wes by ProteinSimple as well as the microchip gel electrophoresis system LabChip® GXII Touch™ HT by PerkinElmer were tested for precision and repeatability compared to SDS‐PAGE (Bio‐Rad). For assessing these quality control parameters, standard model proteins with minor post‐translational modifications were used. Overall, it can be concluded that the CE‐SDS‐based methods are similar to SDS‐PAGE with respect to these parameters. Quality characteristics of test systems gain more significance by testing proteins that do not behave like model proteins. Therefore, glycosylated proteins were analyzed to comparatively investigate the influence of glycosylation on Mr determination in the different instruments. In some cases, high deviations were found both among the methods and with regard to reference values. This article provides possible explanations for these findings.
Keywords	biopharmaceuticals ; comparative study ; gels ; glycosylation ; microchip technology ; molecular weight ; polyacrylamide gel electrophoresis ; quality control
Language	English
Dates of publication	2021-08
Size	p. 1521-1531.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202100068
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Article ; Online: Protein analysis and stability: Overcoming trial-and-error by grouping according to physicochemical properties.

Wätzig, Hermann / Hoffstedt, Marc / Krebs, Finja / Minkner, Robert / Scheller, Christin / Zagst, Holger

Journal of chromatography. A

2021 Volume 1649, Page(s) 462234

Abstract: Today proteins are possibly the most important class of substances. Yet new tasks for proteins are still often solved by trial-and-error approaches. However, in some areas these euphemistically called "screening approaches" are not suitable. E.g. ... ...

Abstract	Today proteins are possibly the most important class of substances. Yet new tasks for proteins are still often solved by trial-and-error approaches. However, in some areas these euphemistically called "screening approaches" are not suitable. E.g. stability tests just take too long and therefore require a more strategic, target-orientated concept. This concept is available by grouping proteins according to their physicochemical properties and then pulling out the right drawer for new tasks. These properties include size, then charge and hydrophobicity as well as their patchinesses, and the degree of order. In addition, solubility, the content of (free) enthalpy, aromatic-amino-acid- and α/β-frequency as well as helix capping, and corresponding patchiness, the number of specific motifs and domains as well as the typical concentration range can be helpful to discriminate between different groups of proteins. Analyzing correlations will reduce the necessary amount of parameters and additional ones, which may be still undiscovered at the present time, can be identified looking at protein subgroups with similar physicochemical properties which still behave heterogeneously. Step-by-step the methodology will be improved. Possibly protein stability will be the driver of this process, but all other areas such as production, purification and analytics including sample pre-treatment and the choice of appropriate separation conditions for e.g. chromatography and electrophoresis will profit from a rational strategy.
MeSH term(s)	Amino Acids/analysis ; Chromatography, Liquid/methods ; Hydrophobic and Hydrophilic Interactions ; Mass Spectrometry/methods ; Proteins/analysis ; Proteins/chemistry ; Solubility ; Thermodynamics
Chemical Substances	Amino Acids ; Proteins
Language	English
Publishing date	2021-05-07
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	1171488-8
ISSN	1873-3778 ; 0021-9673
ISSN (online)	1873-3778
ISSN	0021-9673
DOI	10.1016/j.chroma.2021.462234
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Article ; Online: A comparative study of CE-SDS, SDS-PAGE, and Simple Western-Precision, repeatability, and apparent molecular mass shifts by glycosylation.

Scheller, Christin / Krebs, Finja / Wiesner, Rebecca / Wätzig, Hermann / Oltmann-Norden, Imke

Electrophoresis

2021 Volume 42, Issue 14-15, Page(s) 1521–1531

Abstract	SDS gel electrophoresis is a commonly used approach for monitoring purity and apparent molecular mass (Mr) of proteins, especially in the field of quality control of biopharmaceutical proteins. The technological installation of CE-SDS as the replacement of the slab gel technique (SDS-PAGE) is still in progress, leading to a continuous improvement of CE-SDS instruments. Various CE-SDS instruments, namely Maurice (CE-SDS/CE-SDS PLUS) and Wes by ProteinSimple as well as the microchip gel electrophoresis system LabChip® GXII Touch™ HT by PerkinElmer were tested for precision and repeatability compared to SDS-PAGE (Bio-Rad). For assessing these quality control parameters, standard model proteins with minor post-translational modifications were used. Overall, it can be concluded that the CE-SDS-based methods are similar to SDS-PAGE with respect to these parameters. Quality characteristics of test systems gain more significance by testing proteins that do not behave like model proteins. Therefore, glycosylated proteins were analyzed to comparatively investigate the influence of glycosylation on Mr determination in the different instruments. In some cases, high deviations were found both among the methods and with regard to reference values. This article provides possible explanations for these findings.
MeSH term(s)	Electrophoresis, Capillary ; Electrophoresis, Microchip ; Electrophoresis, Polyacrylamide Gel ; Glycosylation ; Molecular Weight ; Proteins
Chemical Substances	Proteins
Language	English
Publishing date	2021-05-16
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202100068
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Article ; Online: Isoelectric point determination by imaged CIEF of commercially available SARS-CoV-2 proteins and the hACE2 receptor.

Krebs, Finja / Scheller, Christin / Grove-Heike, Kristina / Pohl, Lena / Wätzig, Hermann

Electrophoresis

2021 Volume 42, Issue 6, Page(s) 687–692

Abstract: In order to contribute to the scientific research on the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), we have investigated the isoelectric points (pI) of several related proteins, which are commercially available: the receptor-binding ... ...

Abstract	In order to contribute to the scientific research on the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), we have investigated the isoelectric points (pI) of several related proteins, which are commercially available: the receptor-binding domain (RBD) with His- and Fc-tag, the S1 subunit with His-tag, the S1/S2 subunits with His-tag and the human angiotensin-converting enzyme 2 (hACE2) with His-tag. First, the theoretical pI values, based on the amino acid (AA) sequences of the proteins, were calculated using the ProtParam tool from the Bioinformatics Resource Portal ExPASy. The proteins were then measured with the Maurice imaged CIEF system (native fluorescence detection), testing various measurement conditions, such as different ampholytes or ampholyte mixtures. Due to isoforms, we get sections with several peaks and not just one peak for each protein. The determined pI range for the RBD/Fc is 8.24-9.32 (theoretical pI: 8.55), for the RBD/His it is 7.36-9.88 (8.91) and for the S1/His it is 7.30-8.37 (7.80). The pI range of the S1/S2/His is 4.41-5.87 (no theoretical pI, AA sequence unknown) and for hACE2/His, the determined global range is 5.19-6.11 (5.60) for all experimental conditions chosen. All theoretically derived values were found within these ranges, usually close to the center. Therefore, we consider theoretical values as useful to make predictions about the isoelectric points of SARS-CoV-2 proteins. The experimental conditions had only a minor influence on the pI ranges obtained and mainly influenced the peak shapes.
MeSH term(s)	Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Binding Sites ; COVID-19/metabolism ; COVID-19/virology ; Humans ; Isoelectric Focusing/methods ; Isoelectric Point ; Protein Interaction Domains and Motifs ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; SARS-CoV-2/chemistry ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Protein Subunits ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2021-02-12
Publishing country	Germany
Document type	Journal Article
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202100015
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Article ; Online: Strategies for capillary electrophoresis: Method development and validation for pharmaceutical and biological applications-Updated and completely revised edition.

Krebs, Finja / Zagst, Holger / Stein, Matthias / Ratih, Ratih / Minkner, Robert / Olabi, Mais / Hartung, Sophie / Scheller, Christin / Lapizco-Encinas, Blanca H / Sänger-van de Griend, Cari / García, Carlos D / Wätzig, Hermann

Electrophoresis

2023 Volume 44, Issue 17-18, Page(s) 1279–1341

Abstract: This review is in support of the development of selective, precise, fast, and validated capillary electrophoresis (CE) methods. It follows up a similar article from 1998, Wätzig H, Degenhardt M, Kunkel A. "Strategies for capillary electrophoresis: method ...

Abstract	This review is in support of the development of selective, precise, fast, and validated capillary electrophoresis (CE) methods. It follows up a similar article from 1998, Wätzig H, Degenhardt M, Kunkel A. "Strategies for capillary electrophoresis: method development and validation for pharmaceutical and biological applications," pointing out which fundamentals are still valid and at the same time showing the enormous achievements in the last 25 years. The structures of both reviews are widely similar, in order to facilitate their simultaneous use. Focusing on pharmaceutical and biological applications, the successful use of CE is now demonstrated by more than 600 carefully selected references. Many of those are recent reviews; therefore, a significant overview about the field is provided. There are extra sections about sample pretreatment related to CE and microchip CE, and a completely revised section about method development for protein analytes and biomolecules in general. The general strategies for method development are summed up with regard to selectivity, efficiency, precision, analysis time, limit of detection, sample pretreatment requirements, and validation.
MeSH term(s)	Electrophoresis, Capillary/methods ; Electrophoresis, Microchip ; Proteins ; Pharmaceutical Preparations
Chemical Substances	Proteins ; Pharmaceutical Preparations
Language	English
Publishing date	2023-08-03
Publishing country	Germany
Document type	Journal Article ; Review ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202300158
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Article: Physicochemical properties of SARS‐CoV‐2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control

Scheller, Christin / Krebs, Finja / Minkner, Robert / Astner, Isabel / Gil‐Moles, Maria / Wätzig, Hermann

Electrophoresis. 2020 July, v. 41, no. 13-14

2020

Abstract: The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, ... ...

Abstract	The material properties of the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) and its proteins are discussed. We review the viral structure, size, rigidity, lipophilicity, isoelectric point, buoyant density and centrifugation conditions, stability against pH, temperature, UV light, gamma radiation, and susceptibility to various chemical agents including solvents and detergents. Possible inactivation, downstream, and formulation conditions are given including suitable buffers and some first ideas for quality‐control methods. This information supports vaccine development and discussion with competent authorities during vaccine approval and is certainly related to drug‐targeting strategies and hygienics. Several instructive tables are given, including the pI and grand average of hydropathicity (GRAVY) of SARS‐CoV‐1 and ‐2 proteins in comparison. SARS‐CoV‐1 and SARS‐CoV‐2 are similar in many regards, so information can often be derived. Both are unusually stable, but sensitive at their lipophilic membranes. However, since seemingly small differences can have strong effects, for example, on immunologically relevant epitope settings, unevaluated knowledge transfer from SARS‐CoV‐1 to SARS‐CoV‐2 cannot be advised. Published knowledge regarding downstream processes, formulations and quality assuring methods is, as yet, limited. However, standard approaches employed for other viruses and vaccines seem to be feasible including virus inactivation, centrifugation conditions, and the use of adjuvants.
Keywords	Severe acute respiratory syndrome coronavirus ; Severe acute respiratory syndrome coronavirus 2 ; centrifugation ; electrophoresis ; epitopes ; gamma radiation ; isoelectric point ; lipophilicity ; pH ; quality control ; temperature ; ultraviolet radiation ; vaccine development ; vaccines ; viral morphology ; viruses
Language	English
Dates of publication	2020-07
Size	p. 1137-1151.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; REVIEW
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202000121
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Article: Isoelectric point determination by imaged CIEF of commercially available SARS‐CoV‐2 proteins and the hACE2 receptor

Krebs, Finja / Scheller, Christin / Grove‐Heike, Kristina / Pohl, Lena / Wätzig, Hermann

Electrophoresis. 2021 Mar., v. 42, no. 6

2021

Abstract: In order to contribute to the scientific research on the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), we have investigated the isoelectric points (pI) of several related proteins, which are commercially available: the receptor‐binding ... ...

Abstract	In order to contribute to the scientific research on the severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2), we have investigated the isoelectric points (pI) of several related proteins, which are commercially available: the receptor‐binding domain (RBD) with His‐ and Fc‐tag, the S1 subunit with His‐tag, the S1/S2 subunits with His‐tag and the human angiotensin‐converting enzyme 2 (hACE2) with His‐tag. First, the theoretical pI values, based on the amino acid (AA) sequences of the proteins, were calculated using the ProtParam tool from the Bioinformatics Resource Portal ExPASy. The proteins were then measured with the Maurice imaged CIEF system (native fluorescence detection), testing various measurement conditions, such as different ampholytes or ampholyte mixtures. Due to isoforms, we get sections with several peaks and not just one peak for each protein. The determined pI range for the RBD/Fc is 8.24–9.32 (theoretical pI: 8.55), for the RBD/His it is 7.36–9.88 (8.91) and for the S1/His it is 7.30–8.37 (7.80). The pI range of the S1/S2/His is 4.41–5.87 (no theoretical pI, AA sequence unknown) and for hACE2/His, the determined global range is 5.19–6.11 (5.60) for all experimental conditions chosen. All theoretically derived values were found within these ranges, usually close to the center. Therefore, we consider theoretical values as useful to make predictions about the isoelectric points of SARS‐CoV‐2 proteins. The experimental conditions had only a minor influence on the pI ranges obtained and mainly influenced the peak shapes.
Keywords	Severe acute respiratory syndrome coronavirus 2 ; amino acids ; bioinformatics ; electrophoresis ; fluorescence ; humans ; isoelectric point ; peptidyl-dipeptidase A
Language	English
Dates of publication	2021-03
Size	p. 687-692.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; JOURNAL ARTICLE
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202100015
Database	NAL-Catalogue (AGRICOLA)

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Article: A comparative study of CE‐SDS, SDS‐PAGE, and Simple Western: Influences of sample preparation on molecular weight determination of proteins

Wiesner, Rebecca / Scheller, Christin / Krebs, Finja / Wätzig, Hermann / Oltmann‐Norden, Imke

Electrophoresis. 2021 Feb., v. 42, no. 3

2021

Abstract: The development of capillary electrophoresis, especially CE‐SDS devices, has led CE‐SDS to become an established tool in a wide range of applications in the analysis of biopharmaceuticals and is increasingly replacing its method of origin, SDS‐PAGE. The ... ...

Abstract	The development of capillary electrophoresis, especially CE‐SDS devices, has led CE‐SDS to become an established tool in a wide range of applications in the analysis of biopharmaceuticals and is increasingly replacing its method of origin, SDS‐PAGE. The goal of this study was to evaluate the comparability of molecular weight (MW) determination especially by CE‐SDS and SDS‐PAGE. For ensuring comparability, model proteins that have little or no posttranslational modifications and an IgG antibody were used. Only a minor influence of sample preparation conditions, including sample buffer, temperature conditions, and different reducing agents on the MW determination were found. In contrast, the selection of the MW marker plays a decisive role in determining the accurate apparent MW of a protein. When using different MW markers, the deviation in MW determination can exceed 10%. Interestingly, CE‐SDS and 10% SDS‐PAGE hardly differ in their trueness of MW determination. The trueness in relation to the reference MW for each protein was calculated. Although the trueness values for the model proteins considered range between 1.00 and 1.11 using CE‐SDS, they range between 0.93 and 1.03 on SDS‐PAGE, depending on the experimental conditions chosen.
Keywords	antibodies ; biopharmaceuticals ; capillary electrophoresis ; comparative study ; molecular weight ; polyacrylamide gel electrophoresis ; temperature
Language	English
Dates of publication	2021-02
Size	p. 206-218.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	NAL-AP-2-clean ; JOURNAL ARTICLE
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.202000199
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