## Abstract Collagen peptide (ColP), which was extracted from fish scale with hot water was mixed with glutaraldehyde (GA) in water in the presence of sodium montmorillonite (MMT), and subsequent heat treatment gave the ColP crosslinked by GA (GAβColP)/MMT composite films. Also, the ColP was chain
The effect of ?-irradiation on collagen molecules, isolated ?-chains, and crosslinked native fibers
β Scribed by Cheung, David T. ;Perelman, Natalya ;Tong, Deborah ;Nimni, Marcel E.
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 494 KB
- Volume
- 24
- Category
- Article
- ISSN
- 0021-9304
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β¦ Synopsis
This study shows how collagen molecules are readily damaged by y-radiation at dosages commonly used for sterilizing biomedical products. At 1 Mrad, while the reported effectiveness of the radiation at such a low dosage to completely sterilize a material is questionable, less damage was caused to the collagen peptide backbone. Above such dosage, however, significant damage was clearly demonstrated with collagen alone and collagen in a chemically crosslinked tissue matrix. The enzyme digestion study showed that the material exposed to a very high dosage of radiation resisted degradation by pronase. However, molecular weight analysis showed a significant number of peptide bonds being cleaved by the radiation which could cause considerable changes in the long-term characteristics of the material. Therefore, tissues exposed to high dosages of y-radiation should be tested for long term functional changes. We want to caution against the usage of the enzyme degradation assay as a universal test for all bioprosthetic derived from biological tissues.
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## Abstract Our objective was to strengthen and stabilize collagen films without the introduction of cytotoxic chemical crosslinkers. We hypothesized that collagen could be rapidly crosslinked with glucose with ultraviolet (UV) irradiation as a catalyst. In theory, UVβgenerated free radicals can ex