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Abbadessa, Anna
Publications (3 of 3) Show all publications
Petre, D.-G., Kucko, N. W., Abbadessa, A., Vermonden, T., Polini, A. & Leeuwenburgh, S. C. G. (2019). Surface functionalization of polylactic acid fibers with alendronate groups does not improve the mechanical properties of fiber-reinforced calcium phosphate cements. Journal of The Mechanical Behavior of Biomedical Materials, 90, 472-483
Open this publication in new window or tab >>Surface functionalization of polylactic acid fibers with alendronate groups does not improve the mechanical properties of fiber-reinforced calcium phosphate cements
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2019 (English)In: Journal of The Mechanical Behavior of Biomedical Materials, ISSN 1751-6161, E-ISSN 1878-0180, Vol. 90, p. 472-483Article in journal (Refereed) Published
Abstract [en]

Calcium phosphate cements (CPCs) are frequently used as synthetic bone substitute, but their intrinsic low fracture toughness impedes their application in highly loaded skeletal sites. However, fibers can be used to reduce the brittleness of these CPCs provided that the affinity between the fibers and cement matrix facilitates the transfer of loads from the matrix to the fibers. The aim of the present work was to improve the interface between hydrophobic polylactic acid (PLA) microfibers and hydrophilic CPC. To this end, calcium-binding alendronate groups were conjugated onto the surface of PLA microfibers via different strategies to immobilize a tunable amount of alendronate onto the fiber surface. CPCs reinforced with PLA fibers revealed toughness values which were up to 50-fold higher than unreinforced CPCs. Nevertheless, surface functionalization of PLA microfibers with alendronate groups did not improve the mechanical properties of fiber-reinforced CPCs.

Place, publisher, year, edition, pages
ELSEVIER SCIENCE BV, 2019
Keywords
Calcium phosphate cements, Reinforcement, Polyester, Affinity, Alendronate
National Category
Medical Biotechnology
Identifiers
urn:nbn:se:kth:diva-244108 (URN)10.1016/j.jmbbm.2018.11.003 (DOI)000457510500052 ()30448561 (PubMedID)2-s2.0-85056481582 (Scopus ID)
Note

QC 20190219

Available from: 2019-02-19 Created: 2019-02-19 Last updated: 2019-02-19Bibliographically approved
Abbadessa, A., Oinonen, P. & Henriksson, G. (2018). Characterization of Two Novel Bio-based Materials from Pulping Process Side Streams: Ecohelix and CleanFlow Black Lignin. BioResources, 13(4), 7606-7627
Open this publication in new window or tab >>Characterization of Two Novel Bio-based Materials from Pulping Process Side Streams: Ecohelix and CleanFlow Black Lignin
2018 (English)In: BioResources, ISSN 1930-2126, E-ISSN 1930-2126, Vol. 13, no 4, p. 7606-7627Article in journal (Refereed) Published
Abstract [en]

The characteristics of two novel types of technical lignin, namely Ecohelix (EH) and CleanFlow black lignin (CFBL), isolated from two different pulping process side streams, were analyzed. EH and CFBL were analyzed in terms of general composition, chemical functionalities, molar mass distribution, and thermal stability. For comparison, two relevant types of commercially available lignosulfonate and kraft lignin were used. The results showed that EH contains a large amount of sulfonated lignin, together with carbohydrates and ash. As such, it can be considered a lignin-carbohydrate hybrid molecule. CFBL was found to contain 91.5% Klason lignin and the lowest amount of carbohydrates (0.3%). EH showed the highest content of aliphatic OH groups (5.44 mmol/g) and CFBL a high content of phenols (4.73 mmol/g). EH had a molecular weight of 31.4 kDa and a sufficient thermal stability. CFBL had the lowest molecular weight (M-w = 2.0 kDa) and thermal stability of all kraft lignins analyzed in this study. These properties highlighted that EH is a suitable building block for material development and that CFBL is a promising material for the production of biofuel and biochemicals.

Place, publisher, year, edition, pages
NORTH CAROLINA STATE UNIV DEPT WOOD & PAPER SCI, 2018
Keywords
Lignin characterization, Lignin-carbohydrate complexes, Laccase, Ultrafiltered lignin, Kraft lignin, Lignosulfonate, RUITER GA, 1992, ANALYTICAL BIOCHEMISTRY, V207, P176 Kendry P, 2002, BIORESOURCE TECHNOLOGY, V83, P55 woko M, 2005, BIOMACROMOLECULES, V6, P3467
National Category
Chemical Sciences
Identifiers
urn:nbn:se:kth:diva-241237 (URN)10.15376/biores.13.4.7606-7627 (DOI)000454215100033 ()
Note

QC 20190116

Available from: 2019-01-16 Created: 2019-01-16 Last updated: 2019-03-18Bibliographically approved
Schuurmans, C. C., Abbadessa, A., Bengtson, M. A., Pletikapic, G., Eral, H. B., Koenderink, G., . . . Vermonden, T. (2018). Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels. Soft Matter, 14(30), 6327-6341
Open this publication in new window or tab >>Complex coacervation-based loading and tunable release of a cationic protein from monodisperse glycosaminoglycan microgels
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2018 (English)In: Soft Matter, ISSN 1744-683X, E-ISSN 1744-6848, Vol. 14, no 30, p. 6327-6341Article in journal (Refereed) Published
Abstract [en]

Glycosaminoglycans (GAGs) are of interest for biomedical applications because of their ability to retain proteins (e.g. growth factors) involved in cell-to-cell signaling processes. In this study, the potential of GAG-based microgels for protein delivery and their protein release kinetics upon encapsulation in hydrogel scaffolds were investigated. Monodisperse hyaluronic acid methacrylate (HAMA) and chondroitin sulfate methacrylate (CSMA) micro-hydrogel spheres (diameters 500-700 μm), were used to study the absorption of a cationic model protein (lysozyme), microgel (de)swelling, intra-gel lysozyme distribution and its diffusion coefficient in the microgels dispersed in buffers (pH 7.4) of varying ionic strengths. Upon incubation in 20 mM buffer, lysozyme was absorbed up to 3 and 4 mg mg−1 dry microspheres for HAMA and CSMA microgels respectively, with loading efficiencies up to 100%. Binding stoichiometries of disaccharide : lysozyme (10.2 : 1 and 7.5 : 1 for HAMA and CSMA, respectively) were similar to those for GAG-lysozyme complex coacervates based on soluble GAGs found in literature. Complex coacervates inside GAG microgels were also formed in buffers of higher ionic strengths as opposed to GAG-lysozyme systems based on soluble GAGs, likely due to increased local anionic charge density in the GAG networks. Binding of cationic lysozyme to the negatively charged microgel networks resulted in deswelling up to a factor 2 in diameter. Lysozyme release from the microgels was dependent on the ionic strength of the buffer and on the number of anionic groups per disaccharide, (1 for HAMA versus 2 for CSMA). Lysozyme diffusion coefficients of 0.027 in HAMA and <0.006 μm2 s−1 in CSMA microgels were found in 170 mM buffer (duration of release 14 and 28 days respectively). Fluorescence Recovery After Photobleaching (FRAP) measurements yielded similar trends, although lysozyme diffusion was likely altered due to the negative charges introduced to the protein through the FITC-labeling resulting in weaker protein-matrix interactions. Finally, lysozyme-loaded CSMA microgels were embedded into a thermosensitive hydrogel scaffold. These composite systems showed complete lysozyme release in ∼58 days as opposed to only 3 days for GAG-free scaffolds. In conclusion, covalently crosslinked methacrylated GAG hydrogels have potential as controlled release depots for cationic proteins in tissue engineering applications.

Place, publisher, year, edition, pages
Royal Society of Chemistry, 2018
Keywords
Carrier sense multiple access, Cell signaling, Complex networks, Diffusion, Enzymes, Gels, Hyaluronic acid, Hydrogels, Ionic strength, Medical applications, Photobleaching, Sulfur compounds, Anionic charge densities, Biomedical applications, Cell-to-cell signaling, Covalently cross-linked, Fluorescence recovery after photobleaching, Protein release kinetics, Thermo-sensitive hydrogel, Tissue engineering applications, Scaffolds (biology)
National Category
Biophysics
Identifiers
urn:nbn:se:kth:diva-236357 (URN)10.1039/c8sm00686e (DOI)000449199000017 ()30024582 (PubMedID)2-s2.0-85051114882 (Scopus ID)
Note

QC 20181106

Available from: 2018-11-06 Created: 2018-11-06 Last updated: 2018-11-28Bibliographically approved

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