Bidirectional Binding Property of High Glycine–Tyrosine Keratin-Associated Protein Contributes to the Mechanical Strength and Shape of Hair

    June 2013 in “ Journal of structural biology ”
    Ryo Matsunaga, Ryota Abe, Daisuke Ishii, Shun‐ichi Watanabe, Masato Kiyoshi, Bernd Nöcker, Masaru Tsuchiya, Kouhei Tsumoto
    Studysummary This study suggests that the mechanical robustness of hair may be enhanced by the binding interactions of keratin-associated proteins, particularly KAP8.1, with intermediate filament proteins. Our plain-language summary of this paper — not a Tressless recommendation.
    The study hypothesized that high glycine-tyrosine keratin-associated proteins (HGT KAPs) contributed to hair's mechanical strength and shape by bridging the head domains of intermediate filaments (IFs) and binding to both IFs and the C-terminus of desmoplakin (DPCT). This was supported by protein interaction analyses, including Western blot, isothermal titration calorimetry (ITC), and circular dichroism (CD), which showed strong binding interactions between HGT KAPs and the head domain of K85, a trichocyte IF protein.
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