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We, therefore, sought to develop techniques for hair shaft protein extraction, identification, and quantitative profiling of different proteins.Non-detergent methods using urea-buffers resulted in relatively low yields of protein (20–27%), although adding 2-mercaptoethanol enhanced the protein yield to 50–67%.Human hair proteins were extracted by detergent and detergent-free techniques.
Much interest has recently been drawn to hair follicle interactions with growth factors, cytokines, neuropeptides, neurotransmitters, hormones, and their roles as a source of stem cells.
However, the hair shafts have not received much attention, despite playing roles in temperature regulation, overall defense and protection from the environment, and aesthetics.
Human hair is laminar-fibrous tissue and an evolutionarily old keratinization product of follicle trichocytes.
Studies on the hair proteome can give new insights into hair function and lead to the development of novel biomarkers for hair in health and disease.
Hair keratins comprise type I and type II keratins, which differ from epithelial keratin in their sulfur content.
Although hairs are mainly composed of keratins, they are very challenging to analyze due to the extensive cross-linking, which prevents solubilization.It is also possible that the human microbiome, which is also present in hair, could interact with and thus affect human hair proteins and peptides.Hair has a high protein content with about 300 proteins identified so far.There is, therefore, a clear interest in studying hair proteins such as keratins and KAPs from quantitative, qualitative, and functional perspectives.Hair keratins are very sturdy and extremely difficult to solubilize, and it remains technically challenging to identify and quantify these proteins accurately.Overcoming these technical challenges is therefore vital for understanding the abundances of keratin and other proteins or peptides, their structures, and their biological roles.Such information could also help to establish possible biomarkers for hair quality and hair diseases.LC-MS/MS analysis of the proteins extracted using urea, SDSI, and SDSII generated 97,833, 100,048, and 98718 spectra, which correspond to 12,000, 23,000 and 20,000 peptides, respectively.Proteomic analysis of human hair samples identified 163.5 ± 16.2, 222.5 ± 12.0 and 198.5 ± 7.7 proteins (urea, SDSI, and SDSII extraction, respectively; Fig. Quantitatively, the SDSI and SDSII extraction techniques yielded significantly higher numbers of proteins (p = 0.002, ANOVA; Fig. This suggests that SDS facilitates hair proteome solubilization.Compared to normal hair without protein extraction (Fig. decrease in thickness, the degree of shrinking, mass depletion, overall damage of the hair shaft surface, number of proteins identified and their abundance, the SDS extraction techniques were more efficient than the urea-based extraction method (Table 1).2a), extracted hair shafts using SDSI, SDSII, and urea extraction showed significant shrinking and depletion of mass (Fig. Human hair proteins identified by LC-MS/MS and their physiochemical properties.