In Vitro Assembly and Structure of Trichocyte Keratin Intermediate Filaments

    Wei He, David Parry, L Jones, William W. Idler, Lyuben N. Marekov, Peter M. Steinert
    TLDR Scientists successfully created mouse hair proteins in the lab, which are stable and similar to natural hair.
    The study investigated the in vitro assembly and structural properties of trichocyte keratin intermediate filaments (IFs), crucial for hair and keratinized tissues. Researchers successfully reconstituted these filaments and found that reducing conditions were essential for optimal assembly, with disulfide bonds playing a key role in stabilizing the structure. The study revealed that molecular alignments in reduced trichocyte IFs were similar to cytokeratins, but oxidation caused realignments matching mature wool structure. Detailed analysis showed that disulfide bond formation during terminal differentiation significantly stabilized the IF structure, enhancing the mechanical stability of hair tissues. These findings provided valuable insights into the molecular architecture and stability of keratin IFs, contributing to the understanding of hair biology and potential implications for hair-related disorders.
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