Effect of UV irradiation on stabilized collagen: Role of chromium(III)

Fathima, Nishter Nishad; Suresh, Raju; Rao, Jonnalagadda Raghava; Nair, Balachandran Unni; Ramasami, T.

doi:10.1016/j.colsurfb.2007.09.006

Cited by 17 publications

(12 citation statements)

References 33 publications

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“…The researcher postulated that photopolymerization of collagen chains occurred, leading to higher molecular weight species. However, direct comparison of results between this and other studies might not be entirely valid since some of the other studies irradiated collagen solutions rather than solids (Fujimori 1965; Cooper and Davidson 1965, 1966; Fathima and others 2008) or used UV‐C (Fujimori 1965; Bhat and Karim 2009), UV‐A (Fathima and others 2008), or broad UV spectra (Cooper and Davidson 1965, 1966) rather than UV‐B radiation.…”

Section: Resultsmentioning

confidence: 88%

“…The formation of higher molecular weight species was consistent with results obtained from SDS‐PAGE (Figure 1). Most previous studies on the effects of UV radiation on collagen (Cooper and Davidson 1965, 1966; Fathima and others 2008) and gelatin (Bhat and Karim 2009) had shown a decrease in viscosity at higher UV doses. The researchers of these studies attributed the viscosity decrease to degradation of protein chains by UV radiation.…”

Section: Resultsmentioning

confidence: 95%

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Ultraviolet‐B Radiation Induced Cross‐linking Improves Physical Properties of Cold‐ and Warm‐Water Fish Gelatin Gels and Films

Otoni

Avena‐Bustillos

Chiou

et al. 2012

Journal of Food Science

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Cold- and warm-water fish gelatin granules were exposed to ultraviolet-B radiation for doses up to 29.7 J/cm(2). Solutions and films were prepared from the granules. Gel electrophoresis and refractive index were used to examine changes in molecular weight of the samples. Also, the gel strength and rheological properties of the solutions as well as the tensile and water vapor barrier properties of the films were characterized. SDS-PAGE and refractive index results indicated cross-linking of gelatin chains after exposure to radiation. Interestingly, UV-B treated samples displayed higher gel strengths, with cold- and warm-water fish gelatin having gel strength increases from 1.39 to 2.11 N and from 7.15 to 8.34 N, respectively. In addition, both gelatin samples exhibited an increase in viscosity for higher UV doses. For gelatin films, the cold-water fish gelatin samples made from irradiated granules showed greater tensile strength. In comparison, the warm-water gelatin films made from irradiated granules had lower tensile strength, but better water vapor barrier properties. This might be due to the UV induced cross-linking in warm-water gelatin that disrupted helical structures.

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Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 95%

Ultraviolet‐B Radiation Induced Cross‐linking Improves Physical Properties of Cold‐ and Warm‐Water Fish Gelatin Gels and Films

Otoni

Avena‐Bustillos

Chiou

et al. 2012

Journal of Food Science

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“…Chronoamperogram shows most of the polymer reduction (90%) occurs within the first 20 s (data not shown). Collagen has a characteristic UV absorption at 210 nm, where peptide bonds absorb 23, 24. After reduction of the polymer, the bath solution was characterized using UV spectroscopy for the presence of collagen.…”

Section: Resultsmentioning

confidence: 99%

“…Collagen has a characteristic UV absorption at 210 nm, where peptide bonds absorb. 23,24 After reduction of the polymer, the bath solution was characterized using UV spectroscopy for the presence of collagen. The UV spectrum did not show any noticeable peak at 210 nm, implying that there was no release of collagen from PEDOT into the bath solution.…”

Section: Chemical Composition Of Pedot/collagen and Stability Of Collmentioning

confidence: 99%

Incorporation of collagen in poly(3,4‐ethylenedioxythiophene) for a bifunctional film with high bio‐ and electrochemical activity

Xiao

Wang

et al. 2009

J Biomedical Materials Res

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Electrochemical polymerization can be used to directly synthesize conducting polymers while incorporating different functional molecules such as proteins for specific applications. There is a need to systematically study the effects of synthetic conditions for a polymer/protein composite on its nanostructure, chem/physical properties, and bioactivities. In this study, collagen, a cell-adhesion protein, was impregnated in poly(3,4-ethylenedioxythiophene) (PEDOT) via galvanostatic electropolymerization, and demonstrated binding with the PEDOT backbone and excellent stability. The polymer polymerized at lower current densities shows good electroactivity. Oxidation level of PEDOT was investigated by Raman spectroscopy. The results show that simple inorganic anions are more readily to be doped into the polymer than the bulky collagen molecules. Scanning electron microscope (SEM) observation reveals that the PEDOT/collagen system has a surface morphology different from those previously studied, exhibiting a network structure with nano-silks interlacing. Optical microscopy examination shows that rat pheochromocytoma (PC12) cells are preferentially seeded on PEDOT/collagen other than PEDOT/LiClO(4), indicating that collagen is highly bioactive for cell adhesion. Further study shows that synthesis with a lower current density favors the incorporation of collagen and thus increases the cell attachment to the PEDOT/collagen matrix. This study renders a simple approach to tailor a bifunctional film with high bio- and electrochemical activity.

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“…The fluorescence emission spectra of collagen hydrogels are shown in Figure 6 and a peak at 308 nm were observed. The fluorescence emission of collagen is predominantly ascribed to tyrosine present in polypeptide chains 37, 38. It is clear that there is a gradual decrease in the emission at 308 nm with the increasing absorbed dose when the excitation wavelength is 270 nm.…”

Section: Resultsmentioning

confidence: 99%

Structural study and preliminary biological evaluation on the collagen hydrogel crosslinked by γ‐irradiation

Zhang

Huang

et al. 2012

J Biomedical Materials Res

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Under γ‐irradiation, concentrated collagen solutions yielded collagen hydrogels and liquid products. The molecular structure of collagen hydrogels and the source of the liquid products were studied. Furthermore, preliminary biological properties of the hydrogels were investigated. The results revealed that crosslinking occurred to form collagen hydrogel and the crosslinking density increased with the increasing of the absorbed dose, and the collagen hydrogels showed enhanced mechanical properties. Meanwhile, collagen underwent radiation degradation and water was squeezed out from hydrogel by contraction of hydrogel, yielding liquid products. Collagen hydrogels induced by γ‐irradiation maintained the backbone structure of collagen, and tyrosine partially involved in crosslinking. The irradiated collagen hydrogels have higher denatured temperature, can promote fibroblasts proliferation, and their degradation rate in vivo depended on the absorbed dose. The comprehensive results suggested that the collagen hydrogels prepared by radiation crosslinking preserved the triple helical conformation, possessed improved thermal stability and mechanical properties, excellent biocompatibility, which is expected to favor its application as biomaterials. © 2012 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 100A:2960–2969, 2012.

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Effect of UV irradiation on stabilized collagen: Role of chromium(III)

Cited by 17 publications

References 33 publications

Ultraviolet‐B Radiation Induced Cross‐linking Improves Physical Properties of Cold‐ and Warm‐Water Fish Gelatin Gels and Films

Ultraviolet‐B Radiation Induced Cross‐linking Improves Physical Properties of Cold‐ and Warm‐Water Fish Gelatin Gels and Films

Incorporation of collagen in poly(3,4‐ethylenedioxythiophene) for a bifunctional film with high bio‐ and electrochemical activity

Structural study and preliminary biological evaluation on the collagen hydrogel crosslinked by γ‐irradiation

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