• structure–property relationships of meta-kerateine biomaterials derived from human hair

    جزئیات بیشتر مقاله
    • تاریخ ارائه: 1392/01/01
    • تاریخ انتشار در تی پی بین: 1392/01/01
    • تعداد بازدید: 468
    • تعداد پرسش و پاسخ ها: 0
    • شماره تماس دبیرخانه رویداد: -
     the structure–property relationships of kerateine materials were studied by separating crude hair extracts into two protein sub-fractions, referred to as α- and γ-kerateines, followed by their de novo recombination into meta-kerateine hydrogels, sponges and films. the kerateine fractions were characterized using electrophoresis and mass spectrometry, which revealed that the α-fraction contained complexes of type i and type ii keratins and that the γ-fraction was primarily protein fragments of the α-fraction along with three proteins of the kap-1 family. meta-kerateine materials with increased amounts of γ-kerateines showed diminished physical, mechanical and biological characteristics. most notably, materials with higher γ-content formed less elastic and less solid-like hydrogels and sponges that were less hydrolytically stable. in addition, a model biological assay showed that meta-kerateine films with greater amounts of γ-kerateines were less supportive of hepatocyte attachment. investigation into the mechanism of attachment revealed that hepatocyte adhesion to meta-kerateines is not mediated by the β1 integrin subunit, despite the presence of ldv binding motifs within the type i α-keratins. this work to define the role of protein composition on biomaterial function is essential for the optimization of keratin biomaterials for biomedical applications.

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