Desenvolvimento de processo automático para a reticulação progressiva de matrizes de colágeno com glutaraldeído

Góissis, Gilberto; Braile, D M; Giglioti, Aparecida F.

doi:10.1590/s0104-14281999000400016

Cited by 4 publications

(2 citation statements)

References 10 publications

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“…Collagen is a very promising raw material for tissue engineering, however it is easily biodegradable. Crosslinking of collagen-based matrices is an effective method to modify biodegradation rates and to improve mechanical properties [10][11][12] . Chemical crosslinking can result in materials which are permanently crosslinked [13] , and the in vivo degradation rate of these materials may be controlled [14] .…”

Section: Introductionmentioning

confidence: 99%

Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking

2010

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Abstract:In this work, the modifications promoted by alkaline hydrolysis and glutaraldehyde (GA) crosslinking on type I collagen found in porcine skin have been studied. Collagen matrices were obtained from the alkaline hydrolysis of porcine skin, with subsequent GA crosslinking in different concentrations and reaction times. The elastin content determination showed that independent of the treatment, elastin was present in the matrices. Results obtained from in vitro trypsin degradation indicated that with the increase of GA concentration and reaction time, the degradation rate decreased. From thermogravimetry and differential scanning calorimetry analysis it can be observed that the collagen in the matrices becomes more resistant to thermal degradation as a consequence of the increasing crosslink degree. Scanning electron microscopy analysis indicated that after the GA crosslinking, collagen fibers become more organized and well-defined. Therefore, the preparations of porcine skin matrices with different degradation rates, which can be used in soft tissue reconstruction, are viable.

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Section: Introductionmentioning

confidence: 99%

Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking

2010

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“…Utilizou-se como conservantes, glicerina a 98% por 30 dias [8] e glutaraldeído nas concentrações de 0,625%, 1% e 1,5%, em PBS, pH 7,2 por 18 dias, de acordo com [23].…”

Section: Delineamento Experimentalunclassified

Pathological Features of Bovine Pericardium Implanted Into Mice Abdominal Wall after Preservation with Glutaraldehyde or Glycerin

Costa

Silva²,

Andrade

2016

Acta Scientiae. Vet.

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Background: Lately, the use of biological materials has been widely indicated in surgical procedures to restore structure and function of injured tissues. Bioimplants require different conservation techniques; among these, glutaraldehyde preservation stands out owing to its higher antimicrobial efficiency as compared to glycerin. In view of the need to determine a concentration of glutaraldehyde that can act as a biocide but do not cause undesirable tissue reactions, this study aimed to identify and quantify gross and microscopic tissue alterations after implantation of bovine pericardium, which was preserved in various concentrations of glutaraldehyde, in the abdominal wall of mice.Materials, Methods & Results: Fresh pericardia from 18 bovines were fractioned into 1cm2 samples and treated with a 98% glycerin solution for 30 days (control group), or 0.625%, 1%, and 1.5% glutaraldehyde solution for 18 days (experimental groups). An abdominal muscle fragment was excised from each mouse, and a 1-cm2 fragment of preserved pericardium was implanted in the area. Sixty mice (n = 15 per treatment) divided into groups were observed for 7, 14, and 30 days, and five animals from each group were euthanized at each time point for gross and microscopic examination. Fragments of the implants and adjacent skin lesions were harvested, fixed in formalin, and processed for routine histology and microscopic analysis. Both the type of inflammatory infiltrate and the repair process of the tissue response were similar between the groups that received glycerin-preserved pericardium and those that were subjected to pericardium preserved with 0.625% glutaraldehyde. Animals that received 1% glutaraldehyde-preserved implants and were examined 30 days thereafter exhibited a chronic, intense reaction with fibrosis and necrosis of the abdominal wall muscles, as well as calcification and presence of giant cells, when compared to the animals examined at 7 and 14 days in the same treatment group. These changes were also present and more intense in animals that received 1.5% glutaraldehyde-preserved pericardium examined at 14 and 30 days later, with tissue destruction and impaired incorporation of the implant into the adjacent muscle tissue.Discussion: The continuous cell destruction observed in animals treated with implants preserved with 1% or 1.5% glutaraldehyde is a hallmark of chronic inflammation, since several inflammatory cell molecules contribute to this lesion. A cycle is created: continuous degradation sustains inflammation, and inflammatory molecules contribute to the process of cell destruction. Consequently, we conclude that the use of glutaraldehyde at concentrations of 1 or 1.5% is not feasible for preservation of biological materials. Tissue repair was chronologically more effective in the group treated with glycerinpreserved implants, since animals treated with glutaraldehyde-preserved implants needed a longer period to restore due to presence of a persistent inflammatory response, immunogenicity, calcification, and deficient remodeling. The ideal preservative for biological materials should not cause chronic and/or intense inflammatory reaction in order to preserve the implant’s structure and allow its perfect incorporation into the tissue, even if the chosen preservative is flexible and exhibits disinfectant properties. Therefore, we conclude that glutaraldehyde at concentrations of 0.625% to 1% is suitable as a preservative for biomaterials because the tissue reaction it causes is tolerable; additionally, glutaraldehyde at concentrations close to 1% has been described to have sterilizing properties.

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Dielectric relaxation in slightly hydrated bovine tendon collagen

Rizvi

Khan

2006

J. Phys. D: Appl. Phys.

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With an aim to reveal the mechanism of water–protein interaction from the dielectric response of a model fibrous protein, the dielectric constant ε′ and loss factor ε″ have been measured in air dried and vacuum dried samples of bovine tendon collagen in the frequency range 30 Hz–3 MHz and temperature range 30–200 °C. An anomalous low frequency dispersion (LFD) and an intermediate frequency strong α-dispersion peak were the two main dielectric responses observed in the air dried sample. The LFD followed the fractional power law of frequency while the α-dispersion conformed to the Cole–Cole modified Debye equation. These dispersions, respectively, have been attributed to percolation of protons between and within the clusters of hydrogen bonded water molecules bound to polar or ionizable protein components. In the vacuum dried sample, however, a very weak high frequency α2-dispersion peak was observed, which was hidden below the strong α-dispersion in the air dried sample. This peak may be attributed to reorientation of polar components of the collagen molecule.Temperature dependence of the dielectric data shows release of bound water as a four-step process with discrete peaks at 50, 90, 125 and 160 °C. These peaks have been attributed to the onset of the release of adsorbed surface water, water bound to exposed polar sites, water bound to internal polar sites and very strongly bound structural water, respectively.

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Desenvolvimento de processo automático para a reticulação progressiva de matrizes de colágeno com glutaraldeído

Cited by 4 publications

References 10 publications

Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking

Porcine skin as a source of biodegradable matrices: alkaline treatment and glutaraldehyde crosslinking

Pathological Features of Bovine Pericardium Implanted Into Mice Abdominal Wall after Preservation with Glutaraldehyde or Glycerin

Dielectric relaxation in slightly hydrated bovine tendon collagen

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