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• W2737088146 endingPage "e23037" @default.
• W2737088146 startingPage "e23037" @default.
• W2737088146 abstract "In the past two decades, keratin biomaterials have shown impressive results as scaffolds for tissue engineering, wound healing, and nerve regeneration. In addition to its intrinsic biocompatibility, keratin interacts with specific cell receptors eliciting beneficial biochemical cues. However, during extraction from natural sources, such as hair and wool fibers, natural keratins are subject to extensive processing conditions that lead to formation of unwanted by-products. Additionally, natural keratins suffer from limited sequence tunability. Recombinant keratin proteins can overcome these drawbacks while maintaining the desired chemical and physical characteristics of natural keratins. Herein, we present the bacterial expression, purification, and solution characterization of human hair keratins K31 and K81. The obligate heterodimerization of the K31/K81 pair that results in formation of intermediate filaments is maintained in the recombinant proteins. Surprisingly, we have for the first time observed new zero- and one-dimensional nanostructures from homooligomerization of K81 and K31, respectively. Further analysis of the self-assembly mechanism highlights the importance of disulfide crosslinking in keratin self-assembly." @default.
• W2737088146 created "2017-07-31" @default.
• W2737088146 creator A5015443589 @default.
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• W2737088146 date "2017-07-24" @default.
• W2737088146 modified "2023-10-02" @default.
• W2737088146 title "Homo- and heteropolymer self-assembly of recombinant trichocytic keratins" @default.
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• W2737088146 doi "https://doi.org/10.1002/bip.23037" @default.
• W2737088146 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28741310" @default.
• W2737088146 hasPublicationYear "2017" @default.
• W2737088146 type Work @default.

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