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Effect of the sterilization method on the performance of collagen type I on chronic wound parameters in vitro
Author(s) -
Wiegand Cornelia,
Abel Martin,
Ruth Peter,
Wilhelms Tim,
Schulze Daniel,
Norgauer Johannes,
Hipler UtaChristina
Publication year - 2009
Publication title -
journal of biomedical materials research part b: applied biomaterials
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.665
H-Index - 108
eISSN - 1552-4981
pISSN - 1552-4973
DOI - 10.1002/jbm.b.31338
Subject(s) - sterilization (economics) , proteases , wound healing , matrix metalloproteinase , elastase , chemistry , type i collagen , in vitro , chronic wound , biochemistry , biomedical engineering , surgery , medicine , enzyme , pathology , monetary economics , economics , foreign exchange market , foreign exchange
In the treatment of chronic wounds, it is necessary to establish a physiological wound milieu to improve healing. Application of collagen as wound dressing has been described as beneficial as it possesses the ability to reduce elevated levels of proteases, cytokines, and free radicals. Consequently, a wide range of wound dressings based on collagen have been developed. Native collagen is susceptible to alterations because of influences during the production process; to minimize effects on the molecule itself collagen wound dressings are usually aseptically produced. Common sterilization methods (autoclaving, irradiation, and ethylene oxide (EtO) treatment) can induce changes in the protein chemistry and physical properties, potentially affecting the absorption rate, mechanical strength, or performance. In this study, we have evaluated the influence of γ‐ and β‐irradiation as well as EtO sterilization on the binding capacity of collagen type I for selected proteases and cytokines associated with nonhealing wounds. Although a pronounced effect on the physical properties of the collagen was found, there was no significant loss in the binding affinity for polymorphonuclear elastase, matrix metalloproteinase‐2, and interleukin‐1β, or in the antioxidant capacity. © 2009 Wiley Periodicals, Inc. J Biomed Mater Res Part B: Appl Biomater, 2009