1 citations
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June 2014 in “[Thesis]. Manchester, UK: The University of Manchester; 2014.” The study investigated the viscoelastic properties of human hair after chemical modifications, specifically esterification and disulfide reduction with alkylation. Esterification was found to plasticize the hair matrix and affect the stability of intermediate filaments (IFs), with the alkyl chain length influencing plasticizing efficiency. Disulfide reduction and alkylation significantly impacted the matrix by reducing water content-dependent glass transition and IF stability, although hydrophobic interactions at high water content helped maintain IF integrity. Mechanical tests showed some restoration of stability after propylation. The study suggested that hydrophobic interactions play a role in stabilizing hair fibers at higher relative humidities and water contents, and future research could further elucidate the specific effects of these modifications.
19 citations
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March 2013 in “Biology Letters” The study investigated the evolutionary origin of proteins in the toe pads of the tree frog Hyla cinerea, which are crucial for adhesion in arboreal habitats. Researchers identified five alpha keratins as the main structural proteins in these toe pads. Phylogenetic analyses indicated that these keratins originated from different lineages in an early tetrapod ancestor. In mammals, these keratins evolved to become the major types found in hair. The ancestral keratins were likely expressed in areas needing skin reinforcement in early tetrapods and later diverged to support different adaptive structures in amphibians and mammals.
226 citations
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January 2002 in “Biological and Pharmaceutical Bulletin” A new method quickly extracts and identifies proteins from hair and other keratin sources.
38 citations
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October 2011 in “Analytical biochemistry” Hair proteins have weak spots in their α-helical segments.