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Skog, M., Sivlér, P., Steinvall, I., Aili, D., Sjöberg, F. & Elmasry, M. (2019). The Effect of Enzymatic Digestion on Cultured Epithelial Autografts. Cell Transplantation, 28(5), 638-644
Open this publication in new window or tab >>The Effect of Enzymatic Digestion on Cultured Epithelial Autografts
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2019 (English)In: Cell Transplantation, ISSN 0963-6897, E-ISSN 1555-3892, Vol. 28, no 5, p. 638-644Article in journal (Refereed) Published
Abstract [en]

Severe burns are often treated by means of autologous skin grafts, preferably following early excision of the burnt tissue. In the case of, for example, a large surface trauma, autologous skin cells can be expanded in vitro prior to transplantation to facilitate the treatment when insufficient uninjured skin is a limitation. In this study we have analyzed the impact of the enzyme (trypsin or accutase) used for cell dissociation and the incubation time on cell viability and expansion potential, as well as expression of cell surface markers indicative of stemness. Skin was collected from five individuals undergoing abdominal reduction surgery and the epidermal compartment was digested in either trypsin or accutase. Trypsin generally generated more cells than accutase and with higher viability; however, after 7 days of subsequent culture, accutase-digested samples tended to have a higher cell count than trypsin, although the differences were not significant. No significant difference was found between the enzymes in median fluorescence intensity of the analyzed stem cell markers; however, accutase digestion generated significantly higher levels of CD117- and CD49f-positive cells, but only in the 5 h digestion group. In conclusion, digestion time appeared to affect the isolated cells more than the choice of enzyme.

Place, publisher, year, edition, pages
Sage Publications, 2019
Keywords
autografts, cell culture, epithelial cells, keratinocytes, stem cells
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:liu:diva-156422 (URN)10.1177/0963689719833305 (DOI)000477971000013 ()30983404 (PubMedID)
Note

Funding agencies: Integrative Regenerative Medicine (IGEN) center at Linkoping University

Available from: 2019-04-23 Created: 2019-04-23 Last updated: 2019-08-19
Christoffersson, J., Aronsson, C., Jury, M., Selegård, R., Aili, D. & Mandenius, C.-F. (2018). Fabrication of modular hyaluronan-PEG hydrogels to support 3D cultures of hepatocytes in a perfused liver-on-a-chip device. Biofabrication, 11(1), 1-13, Article ID 015013.
Open this publication in new window or tab >>Fabrication of modular hyaluronan-PEG hydrogels to support 3D cultures of hepatocytes in a perfused liver-on-a-chip device
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2018 (English)In: Biofabrication, ISSN 1758-5082, E-ISSN 1758-5090, Vol. 11, no 1, p. 1-13, article id 015013Article in journal (Refereed) Published
Abstract [en]

Liver cell culture models are attractive in both tissue engineering and for development of assays for drug toxicology research. To retain liver specific cell functions, the use of adequate cell types and culture conditions, such as a 3D orientation of the cells and a proper supply of nutrients and oxygen, are critical. In this article, we show how extracellular matrix mimetic hydrogels can support hepatocyte viability and functionality in a perfused liver-on-a-chip device. A modular hydrogel system based on hyaluronan and poly(ethylene glycol) (HA-PEG), modified with cyclooctyne moieties for bioorthogonal strain-promoted alkyne-azide 1, 3-dipolar cycloaddition (SPAAC), was developed, characterized, and compared for cell compatibility to hydrogels based on agarose and alginate. Hepatoma cells (HepG2) formed spheroids with viable cells in all hydrogels with the highest expression of albumin and urea in alginate hydrogels. By including an excess of cyclooctyne in the HA backbone, azide-modified cell adhesion motifs (linear and cyclic RGD peptides) could be introduced in order to enhance viability and functionality of human induced pluripotent stem cell derived hepatocytes (hiPS-HEPs). In the HA-PEG hydrogels modified with cyclic RGD peptides hiPS-HEPs migrated and grew in 3D and showed an increased viability and higher albumin production compared to when cultured in the other hydrogels. This flexible SPAAC crosslinked hydrogel system enabled fabrication of perfused 3D cell culture of hiPS-HEPs and is a promising material for further development and optimization of liver-on-a-chip devices.

Place, publisher, year, edition, pages
Institute of Physics (IOP), 2018
National Category
Cell and Molecular Biology Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy) Cell Biology
Identifiers
urn:nbn:se:liu:diva-154008 (URN)10.1088/1758-5090/aaf657 (DOI)
Available from: 2019-01-22 Created: 2019-01-22 Last updated: 2019-01-22Bibliographically approved
Chen, H., Chen, P., Huang, J., Selegård, R., Platt, M., Palaniappan, A., . . . Liedberg, B. (2016). Detection of Matrilysin Activity Using Polypeptide Functionalized Reduced Graphene Oxide Field-Effect Transistor Sensor. Analytical Chemistry, 88(6), 2994-2998
Open this publication in new window or tab >>Detection of Matrilysin Activity Using Polypeptide Functionalized Reduced Graphene Oxide Field-Effect Transistor Sensor
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2016 (English)In: Analytical Chemistry, ISSN 0003-2700, E-ISSN 1520-6882, Vol. 88, no 6, p. 2994-2998Article in journal (Refereed) Published
Abstract [en]

A novel approach for rapid and sensitive detection of matrilysin (MMP-7, a biomarker involved in the degradation of various macromolecules) based on a polypeptide (JR2EC) functionalized reduced graphene oxide (rGO) field effect transistor (FET) is reported. MMP-7 specifically digests negatively charged JR2EC immobilized on rGO, thereby modulating the conductance of rGO-FET. The proposed assay enabled detection of MMP-7 at clinically relevant concentrations with a limit of detection (LOD) of 10 ng/mL (400 pM), attributed to the significant reduction of the net charge of JR2EC upon digestion by MMP-7. Quantitative detection of MMP-7 in human plasma was further demonstrated with a LOD of 40 ng/mL, illustrating the potential for the proposed methodology for tumor detection and carcinoma diagnostic (e.g., lung cancer and salivary gland cancer). Additionally, excellent specificity of the proposed assay was demonstrated using matrix metallopeptidase 1 (MMP-1), a protease of the same family. With appropriate selection and modification of polypeptides, the proposed assay could be extended for detection of other enzymes with polypeptide digestion capability.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2016
National Category
Physical Sciences
Identifiers
urn:nbn:se:liu:diva-127272 (URN)10.1021/acs.analchem.5b04663 (DOI)000372391500003 ()26887256 (PubMedID)
Note

Funding Agencies|Institute for Sports Research, Nanyang Technological University; MOE-Tier 1 [2014-T1-001-133-01]

Available from: 2016-04-20 Created: 2016-04-19 Last updated: 2019-01-22
Martinsson, E., Shahjamali, M. M., Large, N., Zaraee, N., Zhou, Y., Schatz, G. C., . . . Aili, D. (2016). Influence of Surfactant Bilayers on the Refractive Index Sensitivity and Catalytic Properties of Anisotropic Gold Nanoparticles. Small, 12(3), 330-342
Open this publication in new window or tab >>Influence of Surfactant Bilayers on the Refractive Index Sensitivity and Catalytic Properties of Anisotropic Gold Nanoparticles
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2016 (English)In: Small, ISSN 1613-6810, E-ISSN 1613-6829, Vol. 12, no 3, p. 330-342Article in journal (Refereed) Published
Abstract [en]

Shape-controlled synthesis of gold nanoparticles generally involves the use of surfactants, typically cetyltrimethylammonium (CTAX, X = Cl-, Br-), to regulate the nucleation growth process and to obtain colloidally stable nanoparticles. The surfactants adsorb on the nanoparticle surface making further functionalization difficult and therefore limit their use in many applications. Herein, the influence of CTAX on nanoparticle sensitivity to local dielectric environment changes is reported. It is shown, both experimentally and theoretically, that the CTAX bilayer significantly reduces the refractive index (RI) sensitivity of anisotropic gold nanoparticles such as nanocubes and concave nanocubes, nanorods, and nanoprisms. The RI sensitivity can be increased by up to 40% by removing the surfactant layer from nanoparticles immobilized on a solid substrate using oxygen plasma treatment. This increase compensates for the otherwise problematic decrease in RI sensitivity caused by the substrate effect. Moreover, the removal of the surfactants both facilitates nanoparticle biofunctionalization and significantly improves their catalytic properties. The strategy presented herein is a simple yet effective universal method for enhancing the RI sensitivity of CTAX-stabilized gold nanoparticles and increasing their potential as transducers in nanoplasmonic sensors, as well as in catalytic and biomedical applications.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH, 2016
National Category
Physical Sciences
Identifiers
urn:nbn:se:liu:diva-125149 (URN)10.1002/smll.201502449 (DOI)000368707800006 ()26583756 (PubMedID)
Note

Funding Agencies|Swedish Research Council (VR); Stockholm Brain Institute (SBI); AFOSR [FA9550-12-1-0280]; NSFs MRSEC program at the Materials Research Center of Northwestern University [DMR-1121262]; Singapore Agency for Science, Technology and Research (A*STAR); Nanyang Technological University Postdoctoral Fellowship by Institute of Nano-System Interface Science & Technology (INSIST).

The previous status of this article was Manuscript.

Available from: 2016-02-15 Created: 2016-02-15 Last updated: 2017-11-30Bibliographically approved
Dånmark, S., Aronsson, C. & Aili, D. (2016). Tailoring Supramolecular Peptide-Poly(ethylene glycol) Hydrogels by Coiled Coil Self-Assembly and Self-Sorting. Biomacromolecules, 17(6), 2260-2267
Open this publication in new window or tab >>Tailoring Supramolecular Peptide-Poly(ethylene glycol) Hydrogels by Coiled Coil Self-Assembly and Self-Sorting
2016 (English)In: Biomacromolecules, ISSN 1525-7797, E-ISSN 1526-4602, Vol. 17, no 6, p. 2260-2267Article in journal (Refereed) Published
Abstract [en]

Physical hydrogels are extensively used in a wide range of biomedical applications. However, different applications require hydrogels with different mechanical and structural properties. Tailoring these properties demands exquisite control over the supramolecular peptides with different affinities for dimerization. Four different mechanical properties of hydrogels using de novo designed coiled coil interactions involved. Here we show that it is possible to control the nonorthogonal peptides, designed to fold into four different coiled coil heterodimers with dissociation constants spanning from mu M to pM, were conjugated to star-shaped 4-arm poly(ethylene glycol) (PEG). The different PEG-coiled coil conjugates self-assemble as a result of peptide heterodimerization. Different combinations of PEG peptide conjugates assemble into PEG peptide networks and hydrogels with distinctly different thermal stabilities, supramolecular, and rheological properties, reflecting the peptide dimer affinities. We also demonstrate that it is possible to rationally modulate the self-assembly process by means of thermodynamic self-sorting by sequential additions of nonpegylated peptides. The specific interactions involved in peptide dimerization thus provides means for programmable and reversible self-assembly of hydrogels with precise control over rheological properties, which can significantly facilitate optimization of their overall performance and adaption to different processing requirements and applications.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2016
National Category
Polymer Chemistry
Identifiers
urn:nbn:se:liu:diva-130135 (URN)10.1021/acs.biomac.6b00528 (DOI)000377924800038 ()27219681 (PubMedID)
Note

Funding Agencies|Swedish Research Council [621-2011-4319]; Swedish Foundation for Strategic Research [ICA10-0002]; Linkoping University; Swedish Government Strategic Research Area in Materials Science on Functional Materials at Linkoping University (Faculty Grant SFO-Mat-LiU) [2009 00971]

Available from: 2016-07-12 Created: 2016-07-11 Last updated: 2019-01-22
Koon Lim, S., Sandén, C., Selegård, R., Liedberg, B. & Aili, D. (2016). Tuning Liposome Membrane Permeability by Competitive Peptide Dimerization and Partitioning-Folding Interactions Regulated by Proteolytic Activity. Scientific Reports, 6(21123), 1-9
Open this publication in new window or tab >>Tuning Liposome Membrane Permeability by Competitive Peptide Dimerization and Partitioning-Folding Interactions Regulated by Proteolytic Activity
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2016 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 6, no 21123, p. 1-9Article in journal (Refereed) Published
Abstract [en]

Membrane active peptides are of large interest for development of drug delivery vehicles and therapeutics for treatment of multiple drug resistant infections. Lack of specificity can be detrimental and finding routes to tune specificity and activity of membrane active peptides is vital for improving their therapeutic efficacy and minimize harmful side effects. We describe a de novo designed membrane active peptide that partition into lipid membranes only when specifically and covalently anchored to the membrane, resulting in pore-formation. Dimerization with a complementary peptide efficiently inhibits formation of pores. The effect can be regulated by proteolytic digestion of the inhibitory peptide by the matrix metalloproteinase MMP-7, an enzyme upregulated in many malignant tumors. This system thus provides a precise and specific route for tuning the permeability of lipid membranes and a novel strategy for development of recognition based membrane active peptides and indirect enzymatically controlled release of liposomal cargo.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2016
National Category
Physical Sciences Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-126131 (URN)10.1038/srep21123 (DOI)000370532500002 ()26892926 (PubMedID)
Note

Funding Agencies|Linkoping University; Swedish Research Council (VR); Swedish Foundation for Strategic Research (SSF); Knut and Alice Wallenberg Foundation (KAW); Centre in Nanoscience and Technology (CeNano); Provost Office, NTU

Available from: 2016-03-15 Created: 2016-03-15 Last updated: 2019-01-22
Gormley, A. J., Chandrawati, R., Christofferson, A. J., Loynachan, C., Jumeaux, C., Artzy-Schnirman, A., . . . Stevens, M. M. (2015). Layer-by-Layer Self-Assembly of Polymer Films and Capsules through Coiled-Coil Peptides. Chemistry of Materials, 27(16), 5820-5824
Open this publication in new window or tab >>Layer-by-Layer Self-Assembly of Polymer Films and Capsules through Coiled-Coil Peptides
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2015 (English)In: Chemistry of Materials, ISSN 0897-4756, E-ISSN 1520-5002, Vol. 27, no 16, p. 5820-5824Article in journal (Refereed) Published
Abstract [en]

The layer-by-layer (LbL) technique is a simple and robust process for fabricating functional multilayer thin films. Here, we report the use of de novo designed polypeptides that self-assemble into coiled-coil structures (four-helix bundles) as a driving force for specific multilayer assembly. These pH- (sensitive between pH 4 and 7) and enzyme-responsive polypeptides were conjugated to polymers, and the LbL assembly of the polymer-peptide conjugates allowed the deposition of up to four polymer-peptide layers on planar surfaces and colloidal substrates. Stable hollow capsules were obtained, and by taking advantage of the peptides susceptibility to specific enzymatic cleavage, release of encapsulated cargo within the carriers can be triggered within 2 h in the presence of matrix metalloproteinase-7. The enormous diversity of materials that can form highly controllable and programmable coiled-coil interactions creates new opportunities and allows further exploration of the multilayer assembly and the formation of carrier capsules with unique functional properties.

Place, publisher, year, edition, pages
AMER CHEMICAL SOC, 2015
National Category
Physical Sciences
Identifiers
urn:nbn:se:liu:diva-121436 (URN)10.1021/acs.chemmater.5b02514 (DOI)000360323700045 ()
Note

Funding Agencies|Whitaker International Scholarship; EPSRC [EP/K020641/1]; Australian Research Council [DP140101888]; Foundation for Strategic Research (SSF); Swedish Research Council (VR)

Available from: 2015-09-18 Created: 2015-09-18 Last updated: 2017-12-04
Gudlur, S., Sandén, C., Matouskova, P., Fasciani, C. & Aili, D. (2015). Liposomes as nanoreactors for the photochemical synthesis of gold nanoparticles. Journal of Colloid and Interface Science, 456, 206-209
Open this publication in new window or tab >>Liposomes as nanoreactors for the photochemical synthesis of gold nanoparticles
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2015 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 456, p. 206-209Article in journal (Refereed) Published
Abstract [en]

A simple and novel method for the photochemical synthesis of AuNPs in liposomes is described. Gold salt is co-encapsulated with the photoinitiator Irgacure-2959 in POPC liposomes prepared via traditional thin-film hydration technique. UVA irradiation for 15 min results in encapsulated AuNPs of 2.8 +/- 1.6 nm in diameter that are primarily dispersed in the aqueous interior of the liposomes. (C) 2015 Elsevier Inc. All rights reserved.

Place, publisher, year, edition, pages
Elsevier, 2015
Keywords
Liposomes; AuNPs; Nanoreactors
National Category
Clinical Medicine Physical Sciences
Identifiers
urn:nbn:se:liu:diva-120718 (URN)10.1016/j.jcis.2015.06.033 (DOI)000358458500027 ()26125517 (PubMedID)
Note

Funding Agencies|Swedish Foundation for Strategic Research (SSF); Center for Integrative Regenerative Medicine (IGEN) at Linkoping University

Available from: 2015-08-24 Created: 2015-08-24 Last updated: 2018-08-22
Wickham, A., Sjölander, D., Bergström, G., Wang, E., Rajendran, V., Hildesjö, C., . . . Aili, D. (2015). Near-Infrared Emitting and Pro-Angiogenic Electrospun Conjugated Polymer Scaffold for Optical Biomaterial Tracking. Advanced Functional Materials, 25(27), 4274-4281
Open this publication in new window or tab >>Near-Infrared Emitting and Pro-Angiogenic Electrospun Conjugated Polymer Scaffold for Optical Biomaterial Tracking
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2015 (English)In: Advanced Functional Materials, ISSN 1616-301X, E-ISSN 1616-3028, Vol. 25, no 27, p. 4274-4281Article in journal (Refereed) Published
Abstract [en]

Noninvasive tracking of biomaterials is vital for determining the fate and degradation of an implant in vivo, and to show its role in tissue regeneration. Current biomaterials have no inherent capacity to enable tracing but require labeling with, for example, fluorescent dyes, or nanoparticles. Here a novel biocompatible fully conjugated electrospun scaffold is described, based on a semiconducting luminescent polymer that can be visualized in situ after implantation using fluorescence imaging. The polymer, poly [2,3-bis-(3-octyloxyphenyl)quinoxaline-5,8-diyl-alt -thiophene-2,5-diyl] (TQ1), is electrospun to form a fibrous mat. The fibers display fluorescence emission in the near-infrared region with lifetimes in the sub-nanosecond range, optimal for in situ imaging. The material shows no cytotoxic behaviors for embryonic chicken cardiomyocytes and mouse myoblasts, and cells migrate onto the TQ1 fibers even in the presence of a collagen substrate. Subcutaneous implantations of the material in rats show incorporation of the TQ1 fibers within the tissue, with limited inflammation and a preponderance of small capillaries around the fibers. The fluorescent properties of the TQ1 fibers are fully retained for up to 90 d following implantation and they can be clearly visualized in tissue using fluorescence and lifetime imaging, thus making it both a pro-angiogenic and traceable biomaterial.

Place, publisher, year, edition, pages
Wiley: 12 months, 2015
Keywords
biomaterials, conjugated polymers, near-infrared, angiogenesis, electrospinning
National Category
Biomaterials Science Polymer Chemistry
Identifiers
urn:nbn:se:liu:diva-120449 (URN)10.1002/adfm.201500351 (DOI)000357996600011 ()
Note

Funding Agencies|Linkoping University; Swedish Foundation for Strategic Research; Swedish Research Council

Available from: 2015-08-12 Created: 2015-08-11 Last updated: 2017-12-04
Aronsson, C., Dånmark, S., Zhou, F., Öberg, P., Enander, K., Su, H. & Aili, D. (2015). Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties. Scientific Reports, 5(14063)
Open this publication in new window or tab >>Self-sorting heterodimeric coiled coil peptides with defined and tuneable self-assembly properties
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2015 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 5, no 14063Article in journal (Refereed) Published
Abstract [en]

Coiled coils with defined assembly properties and dissociation constants are highly attractive components in synthetic biology and for fabrication of peptide-based hybrid nanomaterials and nanostructures. Complex assemblies based on multiple different peptides typically require orthogonal peptides obtained by negative design. Negative design does not necessarily exclude formation of undesired species and may eventually compromise the stability of the desired coiled coils. This work describe a set of four promiscuous 28-residue de novo designed peptides that heterodimerize and fold into parallel coiled coils. The peptides are non-orthogonal and can form four different heterodimers albeit with large differences in affinities. The peptides display dissociation constants for dimerization spanning from the micromolar to the picomolar range. The significant differences in affinities for dimerization make the peptides prone to thermodynamic social self-sorting as shown by thermal unfolding and fluorescence experiments, and confirmed by simulations. The peptides self-sort with high fidelity to form the two coiled coils with the highest and lowest affinities for heterodimerization. The possibility to exploit self-sorting of mutually complementary peptides could hence be a viable approach to guide the assembly of higher order architectures and a powerful strategy for fabrication of dynamic and tuneable nanostructured materials.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2015
National Category
Physical Sciences Electrical Engineering, Electronic Engineering, Information Engineering
Identifiers
urn:nbn:se:liu:diva-121739 (URN)10.1038/srep14063 (DOI)000361177400001 ()26370878 (PubMedID)
Note

Funding Agencies|Swedish Research Council (VR); Swedish Foundation for Strategic Research (SSF)

Available from: 2015-10-06 Created: 2015-10-05 Last updated: 2019-01-22
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-7001-9415

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