Binding Interactions of Keratin-Based Hair Fiber Extract to Gold, Keratin, and BMP-2

    August 2015 in “ PloS one ”
    Roche C. de Guzman, Shanel Tsuda, Minh-Thi N. Ton, Xiao Zhang, Alan R. Esker, Mark Van Dyke
    TLDR Keratin from hair binds well to gold and BMP-2, useful for bone repair.
    The study investigated the binding interactions of keratin-based hair fiber extracts (kerateines) with gold, other kerateines, and bone morphogenetic protein 2 (BMP-2). Kerateines formed a stable 2-nm layer on gold substrates, and their cohesion in neutral water was driven by non-coulombic forces with a dissociation constant (KD) of 1.8 × 10^-4 M. BMP-2 showed a stronger binding to kerateines (KD = 1.1 × 10^-7 M), which weakened in the presence of salts (KD = 3.2 × 10^-5 M). BMP-2 release from kerateine gels was limited (~10% in 4 weeks) and was pH-dependent, with complete dissociation at pH 4.5. These findings highlighted the importance of pH and salt concentration in the binding dynamics, contributing to the development of keratin-based drug delivery systems for bone repair.
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