Joanna Skopińska-Wiśniewska - Academia.edu (original) (raw)
Papers by Joanna Skopińska-Wiśniewska
Materials Science and Engineering: C, Mar 1, 2016
Hydrogels based on collagen and elastin are very valuable materials for medicine and tissue engin... more Hydrogels based on collagen and elastin are very valuable materials for medicine and tissue engineering. They are biocompatible; however their mechanical properties and resistance for enzymatic degradation need to be improved by cross-linking. Up to this point many reagents have been tested but more secure reactants are still sought. Squaric acid (SqAc), 3,4-dihydroxy 3-cyclobutene 1,2-dione, is a strong, cyclic acid, which reacts easily with amine groups. The properties of hydrogels based on collagen/elastin mixtures (95/5, 90/10) containing 5%, 10% and 20% of SqAc and neutralized via dialysis against deionized water were tested. Cross-linked, 3-D, transparent hydrogels were created. The cross-linked materials are stiffer and more resistant to enzymatic degradation than those that are unmodified. The pore size, swelling ability and surface polarity are reduced due to 5% and 10% of SqAc addition. At the same time, the cellular response is not significantly affected by the cross-linking. Therefore, squaric acid would be regarded as a safe, effective cross-linking agent.
Kolagen odgrywa kluczową rolę w utrzymaniu biologicznej i strukturalnej integralności struktury m... more Kolagen odgrywa kluczową rolę w utrzymaniu biologicznej i strukturalnej integralności struktury macierzy zewnątrzkomórkowej i występuje w odmiennych strukturach morfologicznych w różnych tkankach. Skład aminokwasowy kolagenu jest niezwykły dla białek, głównie ze względu na wysoką zawartość hydroksyproliny [1]. Elastyna jest wysoce usieciowanym, nierozpuszczalnym biopolimerem, składającym się z kowalencyjnie związanych cząsteczek tropoelastyny. Posiada ona niezwykły skład aminokwasowy, bo aż 75% jej zawartości stanowią aminokwasy hydrofobowe: glicyna, walina i alanina [2]. Materiały białkowe sieciuje się, w celu poprawienia ich właściwości fizycznych, chemicznych oraz mechanicznych [3]. Skrobia dialdehydowa stanowi polimeryczny dialdehyd wytwarzany na skutek selektywnego utleniania skrobi nadjodanem, który rozszczepia wiązanie C2-C3 łańcucha polisacharydowego skrobi z wytworzeniem dwóch grup aldehydowych [4]. Pektyna jest polisacharydem składającym się głównie z reszt kwasu D-galakturonowego, zestryfikowanych grupami metylowymi [5]. Celem pracy było określenie efektywności sieciowania materiałów kolagenowych oraz kolagenowo-elastynowych przy użyciu skrobi dialdehydowej i pektyny oraz uzyskanie materiałów dla zastosowań w inżynierii tkankowej. Autorzy pragną podziękować Narodowemu Centrum Nauki (NCN, Polska, Grant nr: UMO-2011/03/D/ST8/04600) za zapewnienie wsparcia finansowego na realizację tego projektu.
Introduction. Collagen is the main structural protein of the various connective tissues in mammal... more Introduction. Collagen is the main structural protein of the various connective tissues in mammals. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin. The amino acid composition of collagen is unusual for proteins, mostly because of its high hydroxyproline content. Elastin is a protein which can be mostly found in connective tissues. It is elastic and allows many tissues in the body to resume their shape after stretching or contracting. The chemical composition of elastin is also unusual for proteins, because of desmosine and isodesmosine content. Cross-linking process of the materials was designed to improve its properties, like mechanical strength, porosity and susceptibility to degradation. Aim of the study. The aim of our study was to investigate the influence of dialdehyde starch (DS) and pectin (P) on the properties of collagen/elastin hydrogels. DS is a polysaccharide derived by chemical modification from natural starch. It is prepared by periodate oxidation of starch. Pectin is a complex polysaccharide consisting mainly of esterified D-galacturonic acid resides in an alpha-(1-4) chain. Materials and methods. Collagen was obtained from rat tail tendons. Elastin hydrolysates were isolated from porcine aorta. 1% solution of collagen in 0.1 M acetic acid and 1% solution of elastin hydrolysates in water were prepared. Mixtures of the proteins were prepared in different volume ratios (Coll 100 %; Coll 95%-El 5%; Coll 90 %-El 10%) and were then cross-linked with DS and P. After that, a dialysis against deionised water was performed. Obtained gels were then analysed. Results and conclusions. The FTIR spectra show that the collagen and elastin structure was not changed by cross-linking with dialdehyde starch or pectin. The mechanical properties of the collagen and elastin material cross-linked by DS were improved, while the use of pectin causes deterioration of these properties. The lyophilized gels exhibit porous structure. The various size is observed. The in vitro study demonstrates that the materials are attractive for cells. The addition of dialdehyde starch and pectin causes formation of cross-linking bonds in the collagen and elastin materials and the transparent, hydrogels are obtained. However, the gels containing DS are much stiffer than materials with P. The results show that DS is better cross-linking agent than P. Dialdehyde starch is a suitable cross-linking agent for protein materials for medicine and tissue engineering applications. Acknowledgments. The authors would like to thank the National Science Centre (NCN, Poland, Grant no: UMO-2011/03/D/ST8/04600) for providing financial support to this project
Engineering of Biomaterials, 2010
Engineering of Biomaterials, 2009
Engineering of Biomaterials, 2010
Advanced Structured Materials, 2018
Polymeric microspheres have a wide range of medical and cosmetic applications and synthesis of th... more Polymeric microspheres have a wide range of medical and cosmetic applications and synthesis of these microparticles is the subject of numerous studies. The strategy of incorporating polymer microspheres into three-dimensional matrices to construct controlled-release materials have been attracting increased attention in recent years. The aim of this study was to obtain new materials by means of incorporating polymer microparticles (containing Calendula officinalis flower extract) in the three-dimensional polymer matrix with a porous structure. The microspheres were produced from κ-carrageenan, κ-carrageenan with addition of locust bean gum or sorbitol by extrusion and 2-phase emulsion methods. In the next step, microspheres were incorporated into a collagen/gelatin/hydroxyethyl cellulose matrix and materials were cross-linked using EDC/NHS mixture. The mechanical properties (Young’s modulus) of the obtained materials were characterized. The porous polymeric matrices combined with κ-c...
Engineering of Biomaterials, 2013
Engineering of Biomaterials, 2016
Engineering of Biomaterials, 2011
Molecular Crystals and Liquid Crystals, 2019
The mixtures of hyaluronic acid and poly(vinyl alcohol) were prepared to obtain new bioartificial... more The mixtures of hyaluronic acid and poly(vinyl alcohol) were prepared to obtain new bioartificial materials. HA easily degrades after injection to the human body, so, the mixtures of these polymers can lead to new bioartificial materials with modified degradation behavior. It was also tested whether UV-radiation could be used as a sterilizing agent for these blends. FTIR analysis showed that hydrogen and ester bonds are formed between HA and PVA. The values of surface free energy point out that the polar groups of polymers are involved in the creation of H-bonds. UV-irradiation caused slight changes in surface properties.
Polymers for Advanced Technologies, 2016
Collagen and elastin are the major proteins of an extracellular matrix. They possess attractive, ... more Collagen and elastin are the major proteins of an extracellular matrix. They possess attractive, complementary mechanical properties in their native state, but during isolation, its unique structure is destroyed, which affects the parameters of the materials. However, they still have excellent biological properties. The cross-linking process improves the physicochemical properties of protein materials. The ideal cross-linking agent should be effective and does not impair the biological properties of the material. Therefore, poly(ethylene) glycol-dialdehyde was used in the study. The results show that the addition of poly(ethylene) glycol-dialdehyde in combination with the neutralization of a collagen/elastin solution is a useful method for preparation of protein hydrogels. The gels are transparent and relatively stiff. They exhibit good mechanical properties, surface properties and are attractive for 3 T3 cells.
Journal of Materials Science: Materials in Medicine, 2016
Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical s... more Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical support, strength, and elasticity to various organs and tissues, e.g. skin, tendons, arteries, and bones. They are readily available, biodegradable, biocompatible and they stimulate cell growth. The physicochemical properties of collagen and elastin-based materials can be modified by cross-linking. Glutaraldehyde is one of the most efficient cross-linking agents. However, the unreacted molecules can be released from the material and cause cytotoxic reactions. Thus, the aim of our work was to investigate the influence of a safer, macromolecular cross-linking agentdialdehyde starch (DAS). The properties of hydrogels based on collagen/elastin mixtures (95/5, 90/10) containing 5 and 10 % of DAS and neutralized via dialysis against deionized water were tested. The homogenous, transparent, stiff hydrogels were obtained. The DAS addition causes the formation of intermolecular cross-linking bonds but does not affect the secondary structure of the proteins. As a result, the thermal stability, mechanical strength, and, surprisingly, swelling ability increased. At the same time, the surface properties test and in vitro study show that the materials are attractive for 3T3 cells. Moreover, the materials containing 10 % of DAS are more resistant to enzymatic degradation.
International Journal of Biological Macromolecules, 2015
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the scales of northern pike (E... more Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the scales of northern pike (Esox Lucius) were extracted and characterized. It was the first time that this species was used as sources of collagen. FT-IR and amino acid analysis results revealed the presence of collagen. Glycine accounts for one-third of its amino acid residues and specific for collagen amino acid-hydroxyproline-is present in isolated protein. The content of imino acid: proline and hydroxyproline in ASC and PSC was similar (12.5% Pro and 6.5% Hyp). Both ASC and PSC were type I collagen. The denaturation temperature of ASC and PSC were 28.5 °C and 27 °C, respectively. Thin collagen films were obtained by casting of collagen solution onto glass plates. The surface properties of ASC and PSC films were different-the surface of ASC collagen film was more polar and less rough than PSC and we can observe the formation of collagen fibrils after solvent evaporation. ASC films showed much higher tensile properties than PSC. The obtained results suggest that northern pike scales has potential as an alternative source of collagen for use in various fields.
![Research paper thumbnail of [Comparison of growth of the follicle and mesenchymal stem cells to urothelial cells and fibroblasts on collagen scaffold]](https://attachments.academia-assets.com/116694675/thumbnails/1.jpg)
](Polimery w medycynie, 2008
To develop a tissue-engineered bladder wall replacement with elements obtained from non-urinary t... more To develop a tissue-engineered bladder wall replacement with elements obtained from non-urinary tract components is an atractive idea. The aim of this study was to compare growth of hair follicles epithelial stem cells and mesenchymal stem cells to urothelial cells and fibroblasts cells on scaffold prepared from rat collagen type I. Wistar rats were used in experiment. Rat urothelial cells, hair follicles epithelial stem cells, mesenchymal stem cells and 3T3 cells were cultivated in DMEM (Sigma) supplemented with 10% (or 20% for hair follicles cells) of Fetal Bovine Serum (FBS). Epithelial cell cultures were suplemented with EGF (10 ng/ml; Sigma). Cells were stained using anti-cytokeratine (Clone MMF) and anti-cytokeratine 7. Anti-CD34 and anti-p63 staining were done. Collagen scaffold was prepared from tendoms of Wistar rat's tails. 6-well plates were covered with collagen scaffold. 25 x 10(3) of cells were seeded on each well and cultured for a week. Cells in the controls were...
International Journal of Cosmetic Science, 2011
An investigation into the influence of UV irradiation on keratin hydrolysates was carried out usi... more An investigation into the influence of UV irradiation on keratin hydrolysates was carried out using UV-Vis spectroscopy, Fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. It was found that the absorption of keratin hydrolysates in solution increased during irradiation of the sample, most notably between 250-280 and 320-410 nm. The increase in absorbance in the region 320-410 was because of the new photoproducts formed during UV irradiation of keratin hydrolysates. The fluorescence of keratin hydrolysates was observed at 328 nm after excitation at 270 nm. UV irradiation caused fluorescence fading at 328 nm, and after 60 min of irradiation, a new broad weak band of fluorescence, attributable to new photoproducts, emerged in the UV wavelength region with emission maximum between 400 and 500 nm. FTIR spectroscopy results showed degradation of keratin under UV irradiation. A slight increase in oxidized sulphur species was also observed. The results obtained suggest that UV irradiation can be used as modifying agent for preparation of keratin hydrolysates for cosmetic applications. Ré sumé Comportement physicochimique des hydrolysats de kératine. Une étude concernant l'influence de l'irradiation UV sur des hydrolysats de kératine a été menée en utilisant la spectroscopie UV-Vis, la spectroscopie Infrarouge à transformée de Fourier (FTIR) et la spectroscopie en fluorescence. Lors de l'irradiation de l'échantillon, l'absorption de la solution d'hydrolysats de kératine a augmenté, notamment entre 250-280 nm et 320-410 nm. L'augmentation d'absorbance dans la zone 320-410 nm est liée à la présence de nouveaux photo produits formés pendant l'irradiation UV. La fluorescence des hydrolysats de kératine a été observée à 328 nm suite à une excitation à 270 nm. L'irradiation UV a provoqué la disparition de la fluorescence à 328 nm et après 60 minutes d'irradiation une nouvelle large bande de faible fluorescence, attribuable à de nouveaux photo produits, est apparue dans les longueurs d'ondes UV avec un maximum d'émission entre 400-500 nm. Les résultats de spectroscopie FTIR ont montré une dégradation de kératine sous l'irradiation UV. Une légère augmentation de l'espèce soufre oxydée a aussi été observée. Les résultats obtenus suggèrent que l'irradiation UV peut être utilisée comme agent modifiant les hydrolysats de kératine pour des applications cosmétiques.
International Journal of Photoenergy, 2006
The effect of solar radiation on collagen and collagen/synthetic polymer blends in the form of th... more The effect of solar radiation on collagen and collagen/synthetic polymer blends in the form of thin films and solutions has been studied by UV-VIS and FTIR spectroscopies. Films and solutions of collagen blended with poly(vinyl alcohol) (PVA) and poly(vinyl pyrrolidone) (PVP) were irradiated by solar light. It was found that UV-VIS spectra, which characterize collagen, collagen/PVA, and collagen/PVP blended films, were significantly altered by solar radiation. FTIR spectra of collagen, collagen/PVA, and collagen/PVP films showed that after solar irradiation, the positions of Amide A bands were shifted to lower wavenumbers. There was not any significant alteration in the position of Amide I and Amide II bands of collagen and its blends after solar radiation. The effect of solar UV radiation in comparison with artificial UV radiation has been discussed.
Polymer Degradation and Stability, 2010
The mechanical, thermal and surface properties of chitosan and chitosan containing keratin hydrol... more The mechanical, thermal and surface properties of chitosan and chitosan containing keratin hydrolysates have been studied and the influence of UV irradiation on these properties has been compared. The surface properties of chitosan films containing 5%, 15% and 30% of keratin hydrolysate before and after UV irradiation (l ¼ 254 nm) were investigated by means of contact angle measurements allowing the calculation of surface free energy. The chemical and structural changes during UV irradiation were studied by UVevis and FTIR-ATR spectroscopy. The changes in mechanical properties such as breaking strength, percentage elongation and Young's modulus have been investigated. The results have shown that the mechanical properties of the chitosan/ keratin films were greatly affected by UV irradiation, but the level of the changes of these properties was smaller in the blend than in pure chitosan and strongly dependent on the time of irradiation and composition of the samples. The contact angle and the surface free energy were altered by UV irradiation, which indicates photooxidation and an increase of polarity of specimens. The range of these changes point to greater susceptibility of chitosan to photooxidation in the presence of keratin.
Polymer Degradation and Stability, 2009
The photochemical stability of poly(vinyl alcohol) (PVA) in the presence of 1%, 3% and 5% of coll... more The photochemical stability of poly(vinyl alcohol) (PVA) in the presence of 1%, 3% and 5% of collagen has been studied by Fourier Transform Infrared (FTIR) Spectroscopy, UV-vis spectroscopy, and Differential Scanning Calorimetry (DSC). PVA samples containing 1%, 3% and 5% of collagen were irradiated with UV light wavelength l ¼ 254 nm in air. The results have shown that PVA in the presence of 1%, 3% and 5% of collagen is less stable under UV radiation than pure PVA. A small amount of collagen in PVA enhances photooxidation in the PVA. The amount of crystallinity in PVA containing 1%, 3% and 5% of collagen decreases faster with UV irradiation time than that for pure PVA films.
Materials Science and Engineering: C, Mar 1, 2016
Hydrogels based on collagen and elastin are very valuable materials for medicine and tissue engin... more Hydrogels based on collagen and elastin are very valuable materials for medicine and tissue engineering. They are biocompatible; however their mechanical properties and resistance for enzymatic degradation need to be improved by cross-linking. Up to this point many reagents have been tested but more secure reactants are still sought. Squaric acid (SqAc), 3,4-dihydroxy 3-cyclobutene 1,2-dione, is a strong, cyclic acid, which reacts easily with amine groups. The properties of hydrogels based on collagen/elastin mixtures (95/5, 90/10) containing 5%, 10% and 20% of SqAc and neutralized via dialysis against deionized water were tested. Cross-linked, 3-D, transparent hydrogels were created. The cross-linked materials are stiffer and more resistant to enzymatic degradation than those that are unmodified. The pore size, swelling ability and surface polarity are reduced due to 5% and 10% of SqAc addition. At the same time, the cellular response is not significantly affected by the cross-linking. Therefore, squaric acid would be regarded as a safe, effective cross-linking agent.
Kolagen odgrywa kluczową rolę w utrzymaniu biologicznej i strukturalnej integralności struktury m... more Kolagen odgrywa kluczową rolę w utrzymaniu biologicznej i strukturalnej integralności struktury macierzy zewnątrzkomórkowej i występuje w odmiennych strukturach morfologicznych w różnych tkankach. Skład aminokwasowy kolagenu jest niezwykły dla białek, głównie ze względu na wysoką zawartość hydroksyproliny [1]. Elastyna jest wysoce usieciowanym, nierozpuszczalnym biopolimerem, składającym się z kowalencyjnie związanych cząsteczek tropoelastyny. Posiada ona niezwykły skład aminokwasowy, bo aż 75% jej zawartości stanowią aminokwasy hydrofobowe: glicyna, walina i alanina [2]. Materiały białkowe sieciuje się, w celu poprawienia ich właściwości fizycznych, chemicznych oraz mechanicznych [3]. Skrobia dialdehydowa stanowi polimeryczny dialdehyd wytwarzany na skutek selektywnego utleniania skrobi nadjodanem, który rozszczepia wiązanie C2-C3 łańcucha polisacharydowego skrobi z wytworzeniem dwóch grup aldehydowych [4]. Pektyna jest polisacharydem składającym się głównie z reszt kwasu D-galakturonowego, zestryfikowanych grupami metylowymi [5]. Celem pracy było określenie efektywności sieciowania materiałów kolagenowych oraz kolagenowo-elastynowych przy użyciu skrobi dialdehydowej i pektyny oraz uzyskanie materiałów dla zastosowań w inżynierii tkankowej. Autorzy pragną podziękować Narodowemu Centrum Nauki (NCN, Polska, Grant nr: UMO-2011/03/D/ST8/04600) za zapewnienie wsparcia finansowego na realizację tego projektu.
Introduction. Collagen is the main structural protein of the various connective tissues in mammal... more Introduction. Collagen is the main structural protein of the various connective tissues in mammals. Collagen, in the form of elongated fibrils, is mostly found in fibrous tissues such as tendons, ligaments and skin. The amino acid composition of collagen is unusual for proteins, mostly because of its high hydroxyproline content. Elastin is a protein which can be mostly found in connective tissues. It is elastic and allows many tissues in the body to resume their shape after stretching or contracting. The chemical composition of elastin is also unusual for proteins, because of desmosine and isodesmosine content. Cross-linking process of the materials was designed to improve its properties, like mechanical strength, porosity and susceptibility to degradation. Aim of the study. The aim of our study was to investigate the influence of dialdehyde starch (DS) and pectin (P) on the properties of collagen/elastin hydrogels. DS is a polysaccharide derived by chemical modification from natural starch. It is prepared by periodate oxidation of starch. Pectin is a complex polysaccharide consisting mainly of esterified D-galacturonic acid resides in an alpha-(1-4) chain. Materials and methods. Collagen was obtained from rat tail tendons. Elastin hydrolysates were isolated from porcine aorta. 1% solution of collagen in 0.1 M acetic acid and 1% solution of elastin hydrolysates in water were prepared. Mixtures of the proteins were prepared in different volume ratios (Coll 100 %; Coll 95%-El 5%; Coll 90 %-El 10%) and were then cross-linked with DS and P. After that, a dialysis against deionised water was performed. Obtained gels were then analysed. Results and conclusions. The FTIR spectra show that the collagen and elastin structure was not changed by cross-linking with dialdehyde starch or pectin. The mechanical properties of the collagen and elastin material cross-linked by DS were improved, while the use of pectin causes deterioration of these properties. The lyophilized gels exhibit porous structure. The various size is observed. The in vitro study demonstrates that the materials are attractive for cells. The addition of dialdehyde starch and pectin causes formation of cross-linking bonds in the collagen and elastin materials and the transparent, hydrogels are obtained. However, the gels containing DS are much stiffer than materials with P. The results show that DS is better cross-linking agent than P. Dialdehyde starch is a suitable cross-linking agent for protein materials for medicine and tissue engineering applications. Acknowledgments. The authors would like to thank the National Science Centre (NCN, Poland, Grant no: UMO-2011/03/D/ST8/04600) for providing financial support to this project
Engineering of Biomaterials, 2010
Engineering of Biomaterials, 2009
Engineering of Biomaterials, 2010
Advanced Structured Materials, 2018
Polymeric microspheres have a wide range of medical and cosmetic applications and synthesis of th... more Polymeric microspheres have a wide range of medical and cosmetic applications and synthesis of these microparticles is the subject of numerous studies. The strategy of incorporating polymer microspheres into three-dimensional matrices to construct controlled-release materials have been attracting increased attention in recent years. The aim of this study was to obtain new materials by means of incorporating polymer microparticles (containing Calendula officinalis flower extract) in the three-dimensional polymer matrix with a porous structure. The microspheres were produced from κ-carrageenan, κ-carrageenan with addition of locust bean gum or sorbitol by extrusion and 2-phase emulsion methods. In the next step, microspheres were incorporated into a collagen/gelatin/hydroxyethyl cellulose matrix and materials were cross-linked using EDC/NHS mixture. The mechanical properties (Young’s modulus) of the obtained materials were characterized. The porous polymeric matrices combined with κ-c...
Engineering of Biomaterials, 2013
Engineering of Biomaterials, 2016
Engineering of Biomaterials, 2011
Molecular Crystals and Liquid Crystals, 2019
The mixtures of hyaluronic acid and poly(vinyl alcohol) were prepared to obtain new bioartificial... more The mixtures of hyaluronic acid and poly(vinyl alcohol) were prepared to obtain new bioartificial materials. HA easily degrades after injection to the human body, so, the mixtures of these polymers can lead to new bioartificial materials with modified degradation behavior. It was also tested whether UV-radiation could be used as a sterilizing agent for these blends. FTIR analysis showed that hydrogen and ester bonds are formed between HA and PVA. The values of surface free energy point out that the polar groups of polymers are involved in the creation of H-bonds. UV-irradiation caused slight changes in surface properties.
Polymers for Advanced Technologies, 2016
Collagen and elastin are the major proteins of an extracellular matrix. They possess attractive, ... more Collagen and elastin are the major proteins of an extracellular matrix. They possess attractive, complementary mechanical properties in their native state, but during isolation, its unique structure is destroyed, which affects the parameters of the materials. However, they still have excellent biological properties. The cross-linking process improves the physicochemical properties of protein materials. The ideal cross-linking agent should be effective and does not impair the biological properties of the material. Therefore, poly(ethylene) glycol-dialdehyde was used in the study. The results show that the addition of poly(ethylene) glycol-dialdehyde in combination with the neutralization of a collagen/elastin solution is a useful method for preparation of protein hydrogels. The gels are transparent and relatively stiff. They exhibit good mechanical properties, surface properties and are attractive for 3 T3 cells.
Journal of Materials Science: Materials in Medicine, 2016
Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical s... more Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical support, strength, and elasticity to various organs and tissues, e.g. skin, tendons, arteries, and bones. They are readily available, biodegradable, biocompatible and they stimulate cell growth. The physicochemical properties of collagen and elastin-based materials can be modified by cross-linking. Glutaraldehyde is one of the most efficient cross-linking agents. However, the unreacted molecules can be released from the material and cause cytotoxic reactions. Thus, the aim of our work was to investigate the influence of a safer, macromolecular cross-linking agentdialdehyde starch (DAS). The properties of hydrogels based on collagen/elastin mixtures (95/5, 90/10) containing 5 and 10 % of DAS and neutralized via dialysis against deionized water were tested. The homogenous, transparent, stiff hydrogels were obtained. The DAS addition causes the formation of intermolecular cross-linking bonds but does not affect the secondary structure of the proteins. As a result, the thermal stability, mechanical strength, and, surprisingly, swelling ability increased. At the same time, the surface properties test and in vitro study show that the materials are attractive for 3T3 cells. Moreover, the materials containing 10 % of DAS are more resistant to enzymatic degradation.
International Journal of Biological Macromolecules, 2015
Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the scales of northern pike (E... more Acid soluble collagen (ASC) and pepsin soluble collagen (PSC) from the scales of northern pike (Esox Lucius) were extracted and characterized. It was the first time that this species was used as sources of collagen. FT-IR and amino acid analysis results revealed the presence of collagen. Glycine accounts for one-third of its amino acid residues and specific for collagen amino acid-hydroxyproline-is present in isolated protein. The content of imino acid: proline and hydroxyproline in ASC and PSC was similar (12.5% Pro and 6.5% Hyp). Both ASC and PSC were type I collagen. The denaturation temperature of ASC and PSC were 28.5 °C and 27 °C, respectively. Thin collagen films were obtained by casting of collagen solution onto glass plates. The surface properties of ASC and PSC films were different-the surface of ASC collagen film was more polar and less rough than PSC and we can observe the formation of collagen fibrils after solvent evaporation. ASC films showed much higher tensile properties than PSC. The obtained results suggest that northern pike scales has potential as an alternative source of collagen for use in various fields.
Polimery w medycynie, 2008
To develop a tissue-engineered bladder wall replacement with elements obtained from non-urinary t... more To develop a tissue-engineered bladder wall replacement with elements obtained from non-urinary tract components is an atractive idea. The aim of this study was to compare growth of hair follicles epithelial stem cells and mesenchymal stem cells to urothelial cells and fibroblasts cells on scaffold prepared from rat collagen type I. Wistar rats were used in experiment. Rat urothelial cells, hair follicles epithelial stem cells, mesenchymal stem cells and 3T3 cells were cultivated in DMEM (Sigma) supplemented with 10% (or 20% for hair follicles cells) of Fetal Bovine Serum (FBS). Epithelial cell cultures were suplemented with EGF (10 ng/ml; Sigma). Cells were stained using anti-cytokeratine (Clone MMF) and anti-cytokeratine 7. Anti-CD34 and anti-p63 staining were done. Collagen scaffold was prepared from tendoms of Wistar rat's tails. 6-well plates were covered with collagen scaffold. 25 x 10(3) of cells were seeded on each well and cultured for a week. Cells in the controls were...
International Journal of Cosmetic Science, 2011
An investigation into the influence of UV irradiation on keratin hydrolysates was carried out usi... more An investigation into the influence of UV irradiation on keratin hydrolysates was carried out using UV-Vis spectroscopy, Fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. It was found that the absorption of keratin hydrolysates in solution increased during irradiation of the sample, most notably between 250-280 and 320-410 nm. The increase in absorbance in the region 320-410 was because of the new photoproducts formed during UV irradiation of keratin hydrolysates. The fluorescence of keratin hydrolysates was observed at 328 nm after excitation at 270 nm. UV irradiation caused fluorescence fading at 328 nm, and after 60 min of irradiation, a new broad weak band of fluorescence, attributable to new photoproducts, emerged in the UV wavelength region with emission maximum between 400 and 500 nm. FTIR spectroscopy results showed degradation of keratin under UV irradiation. A slight increase in oxidized sulphur species was also observed. The results obtained suggest that UV irradiation can be used as modifying agent for preparation of keratin hydrolysates for cosmetic applications. Ré sumé Comportement physicochimique des hydrolysats de kératine. Une étude concernant l'influence de l'irradiation UV sur des hydrolysats de kératine a été menée en utilisant la spectroscopie UV-Vis, la spectroscopie Infrarouge à transformée de Fourier (FTIR) et la spectroscopie en fluorescence. Lors de l'irradiation de l'échantillon, l'absorption de la solution d'hydrolysats de kératine a augmenté, notamment entre 250-280 nm et 320-410 nm. L'augmentation d'absorbance dans la zone 320-410 nm est liée à la présence de nouveaux photo produits formés pendant l'irradiation UV. La fluorescence des hydrolysats de kératine a été observée à 328 nm suite à une excitation à 270 nm. L'irradiation UV a provoqué la disparition de la fluorescence à 328 nm et après 60 minutes d'irradiation une nouvelle large bande de faible fluorescence, attribuable à de nouveaux photo produits, est apparue dans les longueurs d'ondes UV avec un maximum d'émission entre 400-500 nm. Les résultats de spectroscopie FTIR ont montré une dégradation de kératine sous l'irradiation UV. Une légère augmentation de l'espèce soufre oxydée a aussi été observée. Les résultats obtenus suggèrent que l'irradiation UV peut être utilisée comme agent modifiant les hydrolysats de kératine pour des applications cosmétiques.
International Journal of Photoenergy, 2006
The effect of solar radiation on collagen and collagen/synthetic polymer blends in the form of th... more The effect of solar radiation on collagen and collagen/synthetic polymer blends in the form of thin films and solutions has been studied by UV-VIS and FTIR spectroscopies. Films and solutions of collagen blended with poly(vinyl alcohol) (PVA) and poly(vinyl pyrrolidone) (PVP) were irradiated by solar light. It was found that UV-VIS spectra, which characterize collagen, collagen/PVA, and collagen/PVP blended films, were significantly altered by solar radiation. FTIR spectra of collagen, collagen/PVA, and collagen/PVP films showed that after solar irradiation, the positions of Amide A bands were shifted to lower wavenumbers. There was not any significant alteration in the position of Amide I and Amide II bands of collagen and its blends after solar radiation. The effect of solar UV radiation in comparison with artificial UV radiation has been discussed.
Polymer Degradation and Stability, 2010
The mechanical, thermal and surface properties of chitosan and chitosan containing keratin hydrol... more The mechanical, thermal and surface properties of chitosan and chitosan containing keratin hydrolysates have been studied and the influence of UV irradiation on these properties has been compared. The surface properties of chitosan films containing 5%, 15% and 30% of keratin hydrolysate before and after UV irradiation (l ¼ 254 nm) were investigated by means of contact angle measurements allowing the calculation of surface free energy. The chemical and structural changes during UV irradiation were studied by UVevis and FTIR-ATR spectroscopy. The changes in mechanical properties such as breaking strength, percentage elongation and Young's modulus have been investigated. The results have shown that the mechanical properties of the chitosan/ keratin films were greatly affected by UV irradiation, but the level of the changes of these properties was smaller in the blend than in pure chitosan and strongly dependent on the time of irradiation and composition of the samples. The contact angle and the surface free energy were altered by UV irradiation, which indicates photooxidation and an increase of polarity of specimens. The range of these changes point to greater susceptibility of chitosan to photooxidation in the presence of keratin.
Polymer Degradation and Stability, 2009
The photochemical stability of poly(vinyl alcohol) (PVA) in the presence of 1%, 3% and 5% of coll... more The photochemical stability of poly(vinyl alcohol) (PVA) in the presence of 1%, 3% and 5% of collagen has been studied by Fourier Transform Infrared (FTIR) Spectroscopy, UV-vis spectroscopy, and Differential Scanning Calorimetry (DSC). PVA samples containing 1%, 3% and 5% of collagen were irradiated with UV light wavelength l ¼ 254 nm in air. The results have shown that PVA in the presence of 1%, 3% and 5% of collagen is less stable under UV radiation than pure PVA. A small amount of collagen in PVA enhances photooxidation in the PVA. The amount of crystallinity in PVA containing 1%, 3% and 5% of collagen decreases faster with UV irradiation time than that for pure PVA films.