• 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: 469
    • 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.

سوال خود را در مورد این مقاله مطرح نمایید :

با انتخاب دکمه ثبت پرسش، موافقت خود را با قوانین انتشار محتوا در وبسایت تی پی بین اعلام می کنم
مقالات جدیدترین رویدادها