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Article: Diffusion-controlled release of the theranostic protein-photosensitizer Azulitox from composite of Fmoc-Phenylalanine Fibrils encapsulated with BSA hydrogels

Favella, Patrizia / Kissmann, Ann-Kathrin / Raber, Heinz Fabian / Kubiczek, Dennis Horst / Bodenberger, Patrick / Bodenberger, Nicholas Emil / Rosenau, Frank

Journal of biotechnology. 2021 Nov. 20, v. 341

2021

Abstract: Hydrogels offer a promising potential for the encapsulation and regulated release of drugs due to their biocompatibility and their tunable properties as materials. Only a limited number of systems and procedures enable the encapsulation of sensitive ... ...

Abstract	Hydrogels offer a promising potential for the encapsulation and regulated release of drugs due to their biocompatibility and their tunable properties as materials. Only a limited number of systems and procedures enable the encapsulation of sensitive proteins. N-terminally fmoc-protected phenylalanine has been shown to self-assemble into a transparent, stable hydrogel It can be considered a supergelator due to the low amount of monomers necessary for hydrogelation (0.1% w/v), making it a good candidate for the encapsulation and stabilization of sensitive proteins. However, application options for this hydrogel are rather limited to those of many other fibril-based materials due to its intrinsic lack of mechanical strength and high susceptibility to changes in environmental conditions. Here, we demonstrate that the stability of a fibrillary system and the resulting release of the protein-photosensitizer Azulitox can be increased by combining the hydrogel with a tightly cross-linked BSA hydrogel. Azulitox is known to display cell-penetrating properties, anti-proliferative activity and has a distinctive fluorescence. Confocal microscopy and fluorescence measurements verified the maintenance of all essential functions of the encapsulated protein. In contrast, the combination of fibrillary and protein hydrogel resulted in a significant stabilization of the matrix and an adjustable release pattern for encapsulated protein.
Keywords	biocompatibility ; biotechnology ; confocal microscopy ; crosslinking ; encapsulation ; fluorescence ; hydrogels ; phenylalanine ; strength (mechanics)
Language	English
Dates of publication	2021-1120
Size	p. 51-62.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	843647-2
ISSN	1873-4863 ; 0168-1656 ; 1389-0352
ISSN (online)	1873-4863
ISSN	0168-1656 ; 1389-0352
DOI	10.1016/j.jbiotec.2021.08.014
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 2299: Show issues

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ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Easy Manipulation of Architectures in Protein-based Hydrogels for Cell Culture Applications.

Bodenberger, Nicholas / Kubiczek, Dennis / Rosenau, Frank

Journal of visualized experiments : JoVE

2017 , Issue 126

Abstract: Hydrogels are recognized as promising materials for cell culture applications due to their ability to provide highly hydrated cell environments. The field of 3D templates is rising due to the potential resemblance of those materials to the natural ... ...

Abstract	Hydrogels are recognized as promising materials for cell culture applications due to their ability to provide highly hydrated cell environments. The field of 3D templates is rising due to the potential resemblance of those materials to the natural extracellular matrix. Protein-based hydrogels are particularly promising because they can easily be functionalized and can achieve defined structures with adjustable physicochemical properties. However, the production of macroporous 3D templates for cell culture applications using natural materials is often limited by their weaker mechanical properties compared to those of synthetic materials. Here, different methods were evaluated to produce macroporous bovine serum albumin (BSA)-based hydrogel systems, with adjustable pore sizes in the range of 10 to 70 µm in radius. Furthermore, a method to generate channels in this protein-based material that are several hundred microns long was established. The different methods to produce pores, as well as the influence of pore size on material properties such as swelling ratio, pH, temperature stability, and enzymatic degradation behavior, were analyzed. Pore sizes were investigated in the native, swollen state of the hydrogels using confocal laser scanning microscopy. The feasibility for cell culture applications was evaluated using a cell-adhesive RGD peptide modification of the protein system and two model cell lines: human breast cancer cells (A549) and adenocarcinomic human alveolar basal epithelial cells (MCF7).
MeSH term(s)	A549 Cells ; Cell Culture Techniques/instrumentation ; Cell Culture Techniques/methods ; Extracellular Matrix/chemistry ; Freeze Drying/methods ; Humans ; Hydrogels/chemistry ; MCF-7 Cells ; Oligopeptides/chemistry ; Serum Albumin, Bovine/chemistry
Chemical Substances	Hydrogels ; Oligopeptides ; Serum Albumin, Bovine (27432CM55Q) ; arginyl-glycyl-aspartic acid (78VO7F77PN)
Language	English
Publishing date	2017-08-04
Publishing country	United States
Document type	Journal Article ; Video-Audio Media
ZDB-ID	2259946-0
ISSN	1940-087X ; 1940-087X
ISSN (online)	1940-087X
ISSN	1940-087X
DOI	10.3791/55813
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Easy manipulation of architectures in protein-based hydrogels for cell culture applications

Bodenberger, Nicholas / Kubiczek, Dennis / Rosenau, Frank

Journal of visualized experiments. 2017 Aug. 04, , no. 126

2017

Abstract	Hydrogels are recognized as promising materials for cell culture applications due to their ability to provide highly hydrated cell environments. The field of 3D templates is rising due to the potential resemblance of those materials to the natural extracellular matrix. Protein-based hydrogels are particularly promising because they can easily be functionalized and can achieve defined structures with adjustable physicochemical properties. However, the production of macroporous 3D templates for cell culture applications using natural materials is often limited by their weaker mechanical properties compared to those of synthetic materials. Here, different methods were evaluated to produce macroporous bovine serum albumin (BSA)-based hydrogel systems, with adjustable pore sizes in the range of 10 to 70 μm in radius. Furthermore, a method to generate channels in this protein-based material that are several hundred microns long was established. The different methods to produce pores, as well as the influence of pore size on material properties such as swelling ratio, pH, temperature stability, and enzymatic degradation behavior, were analyzed. Pore sizes were investigated in the native, swollen state of the hydrogels using confocal laser scanning microscopy. The feasibility for cell culture applications was evaluated using a cell-adhesive RGD peptide modification of the protein system and two model cell lines: human breast cancer cells (A549) and adenocarcinomic human alveolar basal epithelial cells (MCF7).
Keywords	bovine serum albumin ; breast neoplasms ; cell culture ; cell lines ; cellular microenvironment ; confocal laser scanning microscopy ; epithelial cells ; extracellular matrix ; humans ; hydrogels ; mechanical properties ; models ; neoplasm cells ; pH ; peptides ; porosity ; porous media ; synthetic products ; temperature
Language	English
Dates of publication	2017-0804
Size	p. e55813.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/55813
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Diffusion-controlled release of the theranostic protein-photosensitizer Azulitox from composite of Fmoc-Phenylalanine Fibrils encapsulated with BSA hydrogels.

Favella, Patrizia / Kissmann, Ann-Kathrin / Raber, Heinz Fabian / Kubiczek, Dennis Horst / Bodenberger, Patrick / Bodenberger, Nicholas Emil / Rosenau, Frank

Journal of biotechnology

2021 Volume 341, Page(s) 51–62

Abstract	Hydrogels offer a promising potential for the encapsulation and regulated release of drugs due to their biocompatibility and their tunable properties as materials. Only a limited number of systems and procedures enable the encapsulation of sensitive proteins. N-terminally fmoc-protected phenylalanine has been shown to self-assemble into a transparent, stable hydrogel It can be considered a supergelator due to the low amount of monomers necessary for hydrogelation (0.1% w/v), making it a good candidate for the encapsulation and stabilization of sensitive proteins. However, application options for this hydrogel are rather limited to those of many other fibril-based materials due to its intrinsic lack of mechanical strength and high susceptibility to changes in environmental conditions. Here, we demonstrate that the stability of a fibrillary system and the resulting release of the protein-photosensitizer Azulitox can be increased by combining the hydrogel with a tightly cross-linked BSA hydrogel. Azulitox is known to display cell-penetrating properties, anti-proliferative activity and has a distinctive fluorescence. Confocal microscopy and fluorescence measurements verified the maintenance of all essential functions of the encapsulated protein. In contrast, the combination of fibrillary and protein hydrogel resulted in a significant stabilization of the matrix and an adjustable release pattern for encapsulated protein.
MeSH term(s)	Delayed-Action Preparations ; Hydrogels ; Phenylalanine ; Photosensitizing Agents ; Precision Medicine
Chemical Substances	Delayed-Action Preparations ; Hydrogels ; Photosensitizing Agents ; Phenylalanine (47E5O17Y3R)
Language	English
Publishing date	2021-08-28
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	843647-2
ISSN	1873-4863 ; 0168-1656 ; 1389-0352
ISSN (online)	1873-4863
ISSN	0168-1656 ; 1389-0352
DOI	10.1016/j.jbiotec.2021.08.014
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2299: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

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Article ; Online: Polyclonal aptamer libraries as binding entities on a graphene FET based biosensor for the discrimination of apo- and holo-retinol binding protein 4.

Kissmann, Ann-Kathrin / Andersson, Jakob / Bozdogan, Anil / Amann, Valerie / Krämer, Markus / Xing, Hu / Raber, Heinz Fabian / Kubiczek, Dennis H / Aspermair, Patrik / Knoll, Wolfgang / Rosenau, Frank

Nanoscale horizons

2022 Volume 7, Issue 7, Page(s) 770–778

Abstract: Oligonucleotide DNA aptamers represent an emergently important class of binding entities towards as different analytes as small molecules or even whole cells. Without requiring the canonical isolation of individual aptamers following the SELEX process, ... ...

Abstract	Oligonucleotide DNA aptamers represent an emergently important class of binding entities towards as different analytes as small molecules or even whole cells. Without requiring the canonical isolation of individual aptamers following the SELEX process, the focused polyclonal libraries prepared by this
MeSH term(s)	Aptamers, Nucleotide/chemistry ; Aptamers, Nucleotide/genetics ; Aptamers, Nucleotide/metabolism ; Biosensing Techniques/methods ; Graphite/metabolism ; Humans ; Kidney Diseases ; Retinol-Binding Proteins, Plasma
Chemical Substances	Aptamers, Nucleotide ; RBP4 protein, human ; Retinol-Binding Proteins, Plasma ; Graphite (7782-42-5)
Language	English
Publishing date	2022-06-27
Publishing country	England
Document type	Journal Article
ISSN	2055-6764
ISSN (online)	2055-6764
DOI	10.1039/d1nh00605c
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Derivates of the Antifungal Peptide Cm-p5 Inhibit Development of

Kubiczek, Dennis / Raber, Heinz / Gonzalez-García, Melaine / Morales-Vicente, Fidel / Staendker, Ludger / Otero-Gonzalez, Anselmo J / Rosenau, Frank

Antibiotics (Basel, Switzerland)

2020 Volume 9, Issue 7

Abstract: Growth in biofilms as a fascinating and complex microbial lifestyle has become widely accepted as one of the key features of pathogenic microbes, to successfully express their full virulence potential and environmental persistence. This also increases ... ...

Abstract	Growth in biofilms as a fascinating and complex microbial lifestyle has become widely accepted as one of the key features of pathogenic microbes, to successfully express their full virulence potential and environmental persistence. This also increases the threat posed by
Language	English
Publishing date	2020-06-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2681345-2
ISSN	2079-6382
ISSN	2079-6382
DOI	10.3390/antibiotics9070363
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: The Diversity of a Polyclonal FluCell-SELEX Library Outperforms Individual Aptamers as Emerging Diagnostic Tools for the Identification of Carbapenem Resistant Pseudomonas aeruginosa.

Kubiczek, Dennis / Raber, Heinz / Bodenberger, Nicholas / Oswald, Thomas / Sahan, Melis / Mayer, Daniel / Wiese, Sebastian / Stenger, Steffen / Weil, Tanja / Rosenau, Frank

Chemistry (Weinheim an der Bergstrasse, Germany)

2020 Volume 26, Issue 64, Page(s) 14536–14545

Abstract: Textbook procedures require the use of individual aptamers enriched in SELEX libraries which are subsequently chemically synthesized after their biochemical characterization. Here we show that this reduction of the available sequence space of large ... ...

Abstract	Textbook procedures require the use of individual aptamers enriched in SELEX libraries which are subsequently chemically synthesized after their biochemical characterization. Here we show that this reduction of the available sequence space of large libraries and thus the diversity of binding molecules reduces the labelling efficiency and fidelity of selected single aptamers towards different strains of the human pathogen Pseudomonas aeruginosa compared to a polyclonal aptamer library enriched by a whole-cell-SELEX involving fluorescent aptamers. The library outperformed single aptamers in reliable and specific targeting of different clinically relevant strains, allowed to inhibit virulence associated cellular functions and identification of bound cell surface targets by aptamer based affinity purification and mass spectrometry. The stunning ease of this FluCell-SELEX and the convincing performance of the P. aeruginosa specific library may pave the way towards generally new and efficient diagnostic techniques based on polyclonal aptamer libraries not only in clinical microbiology.
MeSH term(s)	Aptamers, Nucleotide ; Carbapenems/chemistry ; Gene Library ; Humans ; Pseudomonas aeruginosa/chemistry ; SELEX Aptamer Technique
Chemical Substances	Aptamers, Nucleotide ; Carbapenems
Language	English
Publishing date	2020-10-15
Publishing country	Germany
Document type	Journal Article
ZDB-ID	1478547-X
ISSN	1521-3765 ; 0947-6539
ISSN (online)	1521-3765
ISSN	0947-6539
DOI	10.1002/chem.202000213
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Lectin-mediated reversible immobilization of human cells into a glycosylated macroporous protein hydrogel as a cell culture matrix.

Bodenberger, Nicholas / Kubiczek, Dennis / Trösch, Laura / Gawanbacht, Ali / Wilhelm, Susanne / Tielker, Denis / Rosenau, Frank

Scientific reports

2017 Volume 7, Issue 1, Page(s) 6151

Abstract: 3D cell culture is a helpful approach to study cell-cell interaction in a native-like environment, but is often limited due the challenge of retrieving cells from the material. In this study, we present the use of recombinant lectin B, a sugar-binding ... ...

Abstract	3D cell culture is a helpful approach to study cell-cell interaction in a native-like environment, but is often limited due the challenge of retrieving cells from the material. In this study, we present the use of recombinant lectin B, a sugar-binding protein with four binding cavities, to enable reversible cell integration into a macroporous protein hydrogel matrix. By functionalizing hydrogel precursors with saccharose, lectin B can both bind to sugar moieties on the cellular surface as well as to the modified hydrogel network. Confocal microscopy and flow cytometry analysis revealed cells to be integrated into the network and to adhere and proliferate. Furthermore, the specificity and reversibility was investigated by using a recombinantly produced yellow fluorescent - lectin B fusion protein and a variety of sugars with diverging affinities for lectin B at different concentrations and elution times. Cells could be eluted within minutes by addition of L-fucose to the cell-loaded hydrogels to make cells available for further analysis.
MeSH term(s)	A549 Cells ; Cell Adhesion ; Cell Culture Techniques/methods ; Cell Proliferation ; Flow Cytometry ; Glycosylation ; Humans ; Hydrogels/chemistry ; Microscopy, Confocal ; Pokeweed Mitogens/chemistry ; Pokeweed Mitogens/metabolism ; Porosity ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Sucrose/metabolism
Chemical Substances	Hydrogels ; Pokeweed Mitogens ; Recombinant Proteins ; lectin B, Phytolacca americana ; Sucrose (57-50-1)
Language	English
Publishing date	2017-07-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-06240-w
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: FluCell-SELEX Aptamers as Specific Binding Molecules for Diagnostics of the Health Relevant Gut Bacterium

Raber, Heinz Fabian / Kubiczek, Dennis Horst / Bodenberger, Nicholas / Kissmann, Ann-Kathrin / D'souza, Deena / Xing, Hu / Mayer, Daniel / Xu, Pengfei / Knippschild, Uwe / Spellerberg, Barbara / Weil, Tanja / Rosenau, Frank

International journal of molecular sciences

2021 Volume 22, Issue 19

Abstract: Based on their unique properties, oligonucleotide aptamers have been named a gift of biological chemistry to life science. We report the development of DNA aptamers as the first high-affinity binding molecules available for fast and rapid labeling of the ...

Abstract	Based on their unique properties, oligonucleotide aptamers have been named a gift of biological chemistry to life science. We report the development of DNA aptamers as the first high-affinity binding molecules available for fast and rapid labeling of the human gut bacterium
MeSH term(s)	Akkermansia ; Alzheimer Disease/microbiology ; Aptamers, Nucleotide/chemistry ; Feces/microbiology ; Gastrointestinal Microbiome ; Humans ; SELEX Aptamer Technique
Chemical Substances	Aptamers, Nucleotide
Language	English
Publishing date	2021-09-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms221910425
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: BSA Hydrogel Beads Functionalized with a Specific Aptamer Library for Capturing

Krämer, Markus / Kissmann, Ann-Kathrin / Raber, Heinz Fabian / Xing, Hu / Favella, Patrizia / Müller, Ingrid / Spellerberg, Barbara / Weil, Tanja / Kubiczek, Dennis / Sihler, Susanne / Ziener, Ulrich / Rosenau, Frank

International journal of molecular sciences

2021 Volume 22, Issue 20

Abstract: Systemic blood stream infections are a major threat to human health and are dramatically increasing worldwide. ...

Abstract	Systemic blood stream infections are a major threat to human health and are dramatically increasing worldwide.
MeSH term(s)	Animals ; Aptamers, Nucleotide/analysis ; Aptamers, Nucleotide/genetics ; Aptamers, Nucleotide/metabolism ; Biosensing Techniques/methods ; Gene Library ; Hemolysis ; Humans ; Hydrogels/chemistry ; Materials Testing ; Microspheres ; Pseudomonas Infections/blood ; Pseudomonas Infections/diagnosis ; Pseudomonas aeruginosa/genetics ; Pseudomonas aeruginosa/isolation & purification ; SELEX Aptamer Technique/methods ; Sepsis/blood ; Sepsis/diagnosis ; Sepsis/microbiology ; Serum/microbiology ; Serum Albumin, Bovine/chemistry ; Sheep ; Ultrafiltration/methods
Chemical Substances	Aptamers, Nucleotide ; Hydrogels ; Serum Albumin, Bovine (27432CM55Q)
Language	English
Publishing date	2021-10-15
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms222011118
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