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In recent years, research on synthetic tissues and tissue platforms for tissue engineering has gained significant attention. This growth in tissue engineering is driven by the need for materials that offer enhanced stability, biocompatibility, reduced toxicity, lower production costs, and simpler manufacturing processes. For this aim, biomolecule-based polymers, especially proteins, have become the primary materials of choice. Among these, non-toxic keratin proteins are widely used to improve both stability and biocompatibility.Keratin, a fibrous protein that can be extracted from human hair, is an inexpensive and readily available resource. It is frequently used in tissue engineering applications. Human hair serves as an ideal source for keratin extraction. It is not only a waste product but also contains keratin, which accounts for approximately 80% of its total protein content. The high stability of keratin is due to its abundant proline and cysteine amino acid content. Additionally, the formation of hydrogen and disulfide bonds after extraction simplifies the immobilization process. Furthermore, producing biocompatible materials becomes more efficient and reduces potential manufacturing challenges.In this study, urea and sodium sulfide extraction methods were used for keratin isolation, and their effectiveness in keratin extraction was compared. The isolated keratin was characterized using Scanning Electron Microscopy (SEM), Circular Dichroism (CD) spectroscopy, and SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). Urea-extracted keratin is considered a potential biomedical scaffold, cosmetic, and sustainable material due to its enhanced biofunctionality.
Published in: Hacettepe Journal of Biology and Chemistry
Volume 54, Issue 2, pp. 137-139