Self-Assembly of Solubilized Human Hair Keratins

Lai, Hui Ying; Setyawati, Magdiel Inggrid; Ferhan, Abdul Rahim; Divakarla, Shiva Kamini; Chua, Huei Min; Cho, Nam‐Joon; Chrzanowski, Wojciech; Ng, Kee Woei

doi:10.1021/acsbiomaterials.0c01507

Cited by 13 publications

(9 citation statements)

References 37 publications

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“…In the current study, TMT-based quantitative proteomics revealed that 4,994 proteins were obtained in all samples, and 50 proteins were denoted as candidate genes for wool growth based on differential analysis. In addition, the DEPs were associated with keratin filament, peptidase regulator activity, animal organ development, and membrane lipid metabolic process, which has been reported in other species like human (Lai et al, 2021) and goat (Gao et al, 2016). Based on KEGG pathway enrichment some pathways related to wool growth and hair follicle development were identified, such as Protein digestion and absorption, Fatty acid biosynthesis, ECMreceptor interaction and PI3K-Akt signaling pathway.…”

Section: Discussionmentioning

confidence: 74%

Integration Analysis of Transcriptome and Proteome Reveal the Mechanisms of Goat Wool Bending

Liu

Ding

Liu³

et al. 2022

Front. Cell Dev. Biol.

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Zhongwei goat is a unique Chinese native goat breed for excellent lamb fur. The pattern of flower spikes of the lamb fur was significantly reduced due to the reduction of the bending of the hair strands with growth. In order to explore the molecular mechanism underlying hair bending with growth, we performed the comprehensive analysis of transcriptome and proteome of skins from 45-days, 108-days and 365-days goat based on TMT-based quantitative proteomics and RNA-seq methods. In the three comparison groups, 356, 592 and 282 differentially expressed proteins (DEPs) were screened, respectively. KEGG pathway analysis indicated that DEPs were significantly enriched in a set of signaling pathways related to wool growth and bending, such as ECM-receptor interaction, PI3K-Akt signaling pathway, PPAR signaling pathway, protein digestion and absorption, and metabolic pathways. In addition, 20 DEPs abundance of goat skin at three development stages were examined by PRM method, which validated the reliability of proteomic data. Among them, KRT and collagen alpha family may play an important role in the development of goat hair follicle and wool bending. COL6A1, COL6A2, CRNN, TNC and LOC102178129 were identified as candidate genes based on combined analysis of transcriptome and proteome data and PRM quantification. Our results identify the differential expressed proteins as well as pathways related to the wool bending of Zhongwei goats and provide a theoretical basis for further revealing the molecular mechanism underlying wool bending of goats.

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Section: Discussionmentioning

confidence: 74%

Integration Analysis of Transcriptome and Proteome Reveal the Mechanisms of Goat Wool Bending

Liu

Ding

Liu³

et al. 2022

Front. Cell Dev. Biol.

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“…In addition, keratin-based biomaterials have an intrinsic ability to support cellular proliferation and can be used as sponges, films, and hydrogels for various biomedical applications. These are all possibilities that, to be explored, require a complete characterization of keratin waste, such as that performed on human hair keratin in [ 36 ]. Those applications should combine the well-known basic properties of the raw material into composites having the merit to offer sufficient mechanical and interface performance, needed for its industrial process.…”

Section: Resultsmentioning

confidence: 99%

Physico-Chemical Characterization of Keratin from Wool and Chicken Feathers Extracted Using Refined Chemical Methods

et al. 2022

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In this work, the characteristic structure of keratin extracted from two different kinds of industrial waste, namely sheep wool and chicken feathers, using the sulfitolysis method to allow film deposition, has been investigated. The structural and microscopic properties have been studied by means of scanning electron microscopy (SEM), Raman spectroscopy, atomic force microscopy (AFM), and infrared (IR) spectroscopy. Following this, small-angle X-ray scattering (SAXS) analysis for intermediate filaments has been performed. The results indicate that the assembly character of the fiber can be obtained by using the most suitable extraction method, to respond to hydration, thermal, and redox agents. The amorphous part of the fiber and medium range structure is variously affected by the competition between polar bonds (reversible hydrogen bonds) and disulfide bonds (DB), the covalent irreversible ones, and has been investigated by using fine structural methods such as Raman and SAXS, which have depicted in detail the intermediate filaments of keratin from the two different animal origins. The preservation of the secondary structure of the protein obtained does offer a potential for further application of the waste-obtained keratin in polymer films and, possibly, biocomposites.

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“…[ 45,46 ] These self‐assemblies of hard keratins or soft (cellular) keratins are typically hetero‐assembly, which requires a type I keratin with its pairing type II keratin. [ 44 ] Our work demonstrated that QTY variant keratins had the characteristics of heterotypic self‐assembly and homotypic self‐assembly, which further improved their uses in more biomedical applications. The native sequences of keratins contain a large amount of cysteine, glycine, and proline, a low content of lysine and methionine, and almost no tryptophan.…”

Section: Discussionmentioning

confidence: 88%

“…The mechanics of these hierarchical composites are controlled by the self-assembly of keratins. [1,44] Besides, the formation of cytoskeletal IF in soft epithelia is also dependent on the assembly of cellular keratins. [45,46] These self-assemblies of hard keratins or soft (cellular) keratins are typically hetero-assembly, which requires a type I keratin with its pairing type II keratin.…”

Section: Discussionmentioning

confidence: 99%

Rational design of water‐soluble, homotypic keratins self‐assembly with enhanced bioactivities

Chen,

Wang,

Deng

et al. 2023

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Recombinant keratins possess strong hemostatic and wound healing properties but suffer from poor water solubility that restricts their bioactivities in biomedical applications. Herein, we report the rational design and synthesis of water‐soluble keratins using a simple methodology named the QTY code. In vitro biophysical analyses and molecular dynamic simulation demonstrated a 200‐fold increase in the water solubility of QTY variant keratins without apparent structural changes compared to native proteins. Homotypic self‐assembly was observed for the first time in recombinant keratins in an aqueous environment, without urea and after QTY modification. Cell and animal experiments showed the in situ gel‐forming capability of QTY variant keratins with superior hemostatic and wound healing activities at the wound sites compared to native recombinant keratins. Our work not only presented a simple and feasible pathway to produce large amounts of water‐soluble keratins using QTY modification but also validated the enhanced self‐assembly, hemostasis, and wound healing properties of these novel keratin species that may open up new venues for biomedical applications.

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Self-Assembly of Solubilized Human Hair Keratins

Cited by 13 publications

References 37 publications

Integration Analysis of Transcriptome and Proteome Reveal the Mechanisms of Goat Wool Bending

Integration Analysis of Transcriptome and Proteome Reveal the Mechanisms of Goat Wool Bending

Physico-Chemical Characterization of Keratin from Wool and Chicken Feathers Extracted Using Refined Chemical Methods

Rational design of water‐soluble, homotypic keratins self‐assembly with enhanced bioactivities

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