Some properties of keratin biomaterials: Kerateines
Abstract
Keratins are a family of structural proteins that can be isolated from a variety of tissues. "Soft" keratins are cytoskeletal elements found in epithelial tissues while protective tissues such as nails, hooves, and hair are composed of "hard" keratins. Hard keratins have been the subject of biomaterials investigations for more than three decades. Numerous methods exist for denaturing these proteins which are characterized by a high sulfur content and extensive disulfide bonding, under either oxidative or reductive conditions, extracting them from tissue and processing them into various physical states such as gels, films, coatings, and fibers. Kerateines or keratoses (oxidatively or reductively derived, respectively), alone or in combination with other biomaterials, have been tested in a small number of systems to demonstrate feasibility for medical applications such as wound healing, bone regeneration, hemostasis, and peripheral nerve repair. These investigations have shown generally good compatibility with cells and tissues, but the focus of prior investigations has been fairly narrow, and as a result there is relatively little published data on the general behavior of keratin biomaterials in biological systems beyond cell culture assays. The goal of this study was to produce a reduced form of keratin biomaterial, kerateine, using a typical and well-published technique, and characterize several aspects of its behavior that may have implications to its general use as a biomaterial. Kerateines were extracted from human hair, fabricated into gels and porous scaffolds, characterized, and placed into biological systems to determine their interactions with cells and tissue. Initially, the proteins were analyzed for molecular weight and amino acid content, as well as their ability to facilitate cell adhesion and proliferation. Crosslinked hydrogels were investigated for their hydrolytic stability in vitro; the micro-architecture and in vivo tissue response of lyophilized gels was also studied. These experiments both confirmed and expanded earlier findings that kerateines demonstrate excellent compatibility in biological systems.
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Wang, J., Hao, S., Luo, T., Yang, Q., & Wang, B. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.07.035 · Cited by 86 · see citing works
Keskin‐Erdogan, Z., Şendemir, A., & Hameş, E. E. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.03.035 · Cited by 85 · see citing works
Visible light crosslinkable human hair keratin hydrogels
Yue, K., Liu, Y., Byambaa, B., Singh, V., Liu, W. H., Li, X., Sun, Y., Zhang, Y. S., Tamayol, A., Zhang, P., et al. (2017) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10077 · Cited by 85 · see citing works
“However, most of previously reported keratin scaffolds rely on network formation via physical interactions and/or spontaneous formation of new disulfide bonds.(18,24) This can be a slow process and thus largely limit the encapsulation of cells within keratinbased scaffolds.”
BackgroundEsparza, Y., Bandara, N., Ullah, A., & Wu, J. (2018) · Materials Science and Engineering C · doi:10.1016/j.msec.2018.04.067 · Cited by 82 · see citing works
Extraction of keratin from waste chicken feathers using sodium sulfide and l-cysteine
Pourjavaheri, F., Pour, S. O., Jones, O. A. H., Smooker, P. M., Brkljača, R., Sherkat, F., Blanch, E. W., Gupta, A. K., & Shanks, R. A. (2019) · Process Biochemistry · doi:10.1016/j.procbio.2019.04.010 · Cited by 84 · see citing works
Kaur, M., Arshad, M., & Ullah, A. (2018) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.7b03380 · Cited by 83 · see citing works
Keratinous Materials as Novel Absorbent Systems for Toxic Pollutants
Ghosh, A., & Collie, S. R. (2014) · Defence Science Journal · doi:10.14429/dsj.64.7319 · Cited by 80 · see citing works
Development of keratin nanoparticles for controlled gastric mucoadhesion and drug release
Cheng, Z., Chen, X., Zhai, D., Gao, F., Guo, T., Li, W., Hao, S., Ji, J., & Wang, B. (2018) · Journal of Nanobiotechnology · doi:10.1186/s12951-018-0353-2 · Cited by 79 · see citing works
“The cysteine sulfur atoms of KTN and KOS is in the form of thiol groups and sulfonic acid groups, respectively [14], which results in different properties of KOS and KTN with respect to mucoadhesion, hydrophilicity, solubility, surface charge and degradation rate [11, 14, 15].”
BackgroundTomblyn, S., Kneller, E. L. P., Walker, S. J., Ellenburg, M. D., Kowalczewski, C. J., Dyke, M. E. V., Burnett, L., & Saul, J. M. (2015) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.33438 · Cited by 78 · see citing works
Sando, L., Kim, M., Colgrave, M. L., Ramshaw, J. A. M., Werkmeister, J. A., & Elvin, C. M. (2010) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32913 · Cited by 78 · see citing works
Review of Alternative Carrier Materials for Ocular Surface Reconstruction
Feng, Y., Borrelli, M., Reichl, S., Schrader, S., & Geerling, G. (2014) · Current Eye Research · doi:10.3109/02713683.2013.853803 · Cited by 75 · see citing works
Smart release of antimicrobial ZnO nanoplates from a pH-responsive keratin hydrogel
Villanueva, M. E., Cuestas, M. L., Pérez, C. J., Orto, V. C. D., & Copello, G. J. (2018) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2018.10.067 · Cited by 75 · see citing works
Injectable keratin hydrogels as hemostatic and wound dressing materials
Tang, A., Li, Y., Yao, Y., Yang, X., Cao, Z., Nie, H., & Yang, G. Y. (2021) · Biomaterials Science · doi:10.1039/d1bm00135c · Cited by 73 · see citing works
Novel wound dressing based on nanofibrous PHBV-keratin mats
Yuan, J., Geng, J., Xing, Z., Shim, K.-J., Han, I., Kim, J., Kang, I., & Shen, J. (2012) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.1653 · Cited by 72 · see citing works
“Keratin can be extracted from different sources, including hair (Reichl, 2009; Hill et al., 2010; Nakamura et al., 2002), wool (Sando et al., 2010) and horn (Srinivasan et al., 2010).”
BackgroundKeratin-based antimicrobial textiles, films, and nanofibers
Dickerson, M. B., Sierra, A. A., Bedford, N. M., Lyon, W. J., Gruner, W. E., Mirau, P. A., & Naik, R. R. (2013) · Journal of Materials Chemistry B · doi:10.1039/c3tb20896f · Cited by 71 · see citing works
Hassan, M. A., Taha, T. H., Hamad, G. M., Hashem, M., Alamri, S., & Mostafa, Y. S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.03.032 · Cited by 70 · see citing works
Hybrid hydrogels based on keratin and alginate for tissue engineering
da Silva, R. S., Singh, R., Sarker, B., Papageorgiou, D. G., Juhasz, J. A., Roether, J. A., Cicha, I., Kaschta, J., Schubert, D. W., Chrissafis, K., et al. (2014) · Journal of Materials Chemistry B · doi:10.1039/c4tb00776j · Cited by 70 · see citing works
Keratin biomaterials augment anti-inflammatory macrophage phenotype in vitro
Waters, M., VandeVord, P. J., & Dyke, M. E. V. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.10.042 · Cited by 70 · see citing works
Development and assessment of kerateine nanoparticles for use as a hemostatic agent
Luo, T., Hao, S., Chen, X., Wang, J., Yang, Q., Wang, Y., Weng, Y., Wei, H., Zhou, J., & Wang, B. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.03.007 · Cited by 68 · see citing works
“The soluble protein samples showed α-and γ-kerateine in the SDS-PAGE and 17 amino acids were detected from the kerateine extracts, which was consistent with the published study [36].”
ResultKeratinases as Versatile Enzymatic Tools for Sustainable Development
Sypka, M., Jodłowska, I., & Białkowska, A. M. (2021) · Biomolecules · doi:10.3390/biom11121900 · Cited by 68 · see citing works
Solubilization of keratins and functional properties of their isolates and hydrolysates
Sinkiewicz, I., Staroszczyk, H., & Śliwińska, A. (2018) · Journal of Food Biochemistry · doi:10.1111/jfbc.12494 · Cited by 68 · see citing works
Management of waste sheep wool as valuable organic substrate in European Union countries
Petek, B., & Logar, R. M. (2020) · Journal of Material Cycles and Waste Management · doi:10.1007/s10163-020-01121-3 · Cited by 66 · see citing works
Biofunctional approaches of wool-based keratin for tissue engineering
Ranjit, E., Hamlet, S. M., George, R., Sharma, A., & Love, R. M. (2021) · Journal of Science Advanced Materials and Devices · doi:10.1016/j.jsamd.2021.10.001 · Cited by 66 · see citing works
Tran, C. D., Prosenc, F., Franko, M., & Benzi, G. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.06.021 · Cited by 66 · see citing works
“For example, as previously reported and also observed in this study, regenerated KER film was found to be too brittle to be reasonably used in any application (Hill et al., 2010, Sando et al., 2010, Vasconcelos and Cavaco-Paulo, 2013 and Verma et al., 2008).”
Baker, H. B., Passipieri, J. A., Siriwardane, M. L., Ellenburg, M. D., Vadhavkar, M., Bergman, C. R., Saul, J. M., Tomblyn, S., Burnett, L., & Christ, G. J. (2017) · Tissue Engineering Part A · doi:10.1089/ten.tea.2016.0457 · Cited by 67 · see citing works
“The keratins can be solubilized through disruption of the disulfide bonds to open the cortex and denature the fibers into constitutive proteins through either an oxidative or reductive process.(39,40) Oxidative extraction yields keratins with altered cysteine residues that can no longer cross-link with other keratins…”
BackgroundBhavsar, P. S., Zoccola, M., Patrucco, A., Montarsolo, A., Rovero, G., & Tonin, C. (2016) · Textile Research Journal · doi:10.1177/0040517516658512 · Cited by 65 · see citing works
“These proteins and amino acids can eventually be refined and used as building blocks for various applications.(9) The alkaline hydrolysis of wool with strong hydroxides such as sodium hydroxide, potassium hydroxide, and suchlike, resulted in breakage of disulfide, peptide, and side-chain amide bonds,”
BackgroundLu, T.-Y., Huang, W.-C., Chen, Y., Baskaran, N., Yu, J., & Wei, Y. (2020) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2020.111258 · Cited by 64 · see citing works
Yang, J., Wang, Z., Liang, X., Wang, W., & Wang, S. (2024) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2024.103155 · Cited by 64 · see citing works
Native and synthetic scaffolds for limbal epithelial stem cell transplantation
Nguyen, K. N., Bobba, S., Richardson, A., Park, M., Watson, S. L., Wakefield, D., & Girolamo, N. D. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.10.037 · Cited by 64 · see citing works
Sustainable and smart keratin hydrogel with pH-sensitive swelling and enhanced mechanical properties
Ramos, M. L. P., González, J. A., Fabián, L., Pérez, C. J., Villanueva, M. E., & Copello, G. J. (2017) · Materials Science and Engineering C · doi:10.1016/j.msec.2017.04.120 · Cited by 63 · see citing works
Closing the Loop with Keratin-Rich Fibrous Materials
Perța-Crișan, S., Ursachi, C. Ș., Gavrilaş, S., Oancea, F., & Munteanu, F. (2021) · Polymers · doi:10.3390/polym13111896 · Cited by 62 · see citing works
“Keratins have also been described the γ-keratins [38].”
BackgroundMethodInfluentialRecent advances in keratin for biomedical applications
Wang, L., Shang, Y., Zhang, J., Yuan, J., & Shen, J. (2023) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2023.103012 · Cited by 62 · see citing works
Advances in Protein-Based Materials: From Origin to Novel Biomaterials
Choi, S. M., Chaudhry, P., Zo, S. M., & Han, S. S. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-0950-2_10 · Cited by 63 · see citing works
The tale of a versatile enzyme: Molecular insights into keratinase for its industrial dissemination
Su, C., Gong, J., Qin, J., Li, H., Li, H., Xu, Z., & Shi, J. (2020) · Biotechnology Advances · doi:10.1016/j.biotechadv.2020.107655 · Cited by 61 · see citing works
An optimal designed experiment for the alkaline hydrolysis of feather keratin
Dąbrowska, M., Sommer, A., Sinkiewicz, I., Taraszkiewicz, A., & Staroszczyk, H. (2021) · Environmental Science and Pollution Research · doi:10.1007/s11356-021-17649-2 · Cited by 61 · see citing works
Transglutaminase‐modified wool keratin film and its potential application in tissue engineering
Cui, L., Gong, J., Fan, X., Wang, P., Wang, Q., & Qiu, Y. (2012) · Engineering in Life Sciences · doi:10.1002/elsc.201100206 · Cited by 59 · see citing works
“[22] produced a typical keratin biomaterial from human hair under reducing conditions and investigated their general chemical, physical, and biological properties.”
BackgroundKowalczewski, C. J., Tombyln, S., Wasnick, D. C., Hughes, M. R., Ellenburg, M. D., Callahan, M. F., Smith, T. L., Van Dyke, M. E., Burnett, L. R., & Saul, J. M. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2013.12.087 · Cited by 58 · see citing works
“, cystine), which results in a stable, crosslinked hydrogel [17].”
Tran, C. D., Prosenc, F., Franko, M., & Benzi, G. (2016) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6b14347 · Cited by 58 · see citing works
“4 structures such as hairs, wools, feathers, nails and horns.(19-28) KER possess amino acid sequences”
BackgroundMethodInfluentialRamya, K. R., Thangam, R., & Madhan, B. (2019) · Process Biochemistry · doi:10.1016/j.procbio.2019.11.015 · Cited by 58 · see citing works
Biomolecule-assisted biogenic synthesis of metallic nanoparticles
Malhotra, S. P. K., & Alghuthaymi, M. A. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823575-1.00011-1 · Cited by 57 · see citing works
Roy, D. C., Tomblyn, S., Burmeister, D. M., Wrice, N. L., Becerra, S. C., Burnett, L., Saul, J. M., & Christy, R. J. (2014) · Advances in Wound Care · doi:10.1089/wound.2014.0576 · Cited by 56 · see citing works
“Keratin proteins extracted from hair include a-keratins, which are a-helical structural proteins, and smaller, globular proteins, termed ckeratins.(18) Keratins can be formulated into a variety of dressing materials including foams, sponges, and hydrogels.”
- Authors
- Hill, P., Brantley, H., & Van Dyke, M.
- Affiliations
- Wake Forest University Health Sciences (US)
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 31
- Issue
- 4
- Pages
- 585-593
- ISSN
- 0142-9612 (ISSN-L)
- OpenAlex
- W2040929841
- Semantic Scholar
- 3a26efc3f607a3b184a2e8582ca693e91361e560
- Cited by
- 349
- References
- 42
- Citations by year
- 2026: 13 · 2025: 13 · 2024: 19 · 2023: 23 · 2022: 29 · 2021: 27 · 2020: 38 · 2019: 22 · 2018: 32 · 2017: 32 · 2016: 27 · 2015: 17 · 2014: 22 · 2013: 13 · 2012: 9
- FWCI
- 3.22
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Biomaterials (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Army
- Errett Fisher Foundation
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Keywords
- keratin, hard keratin, human hair, crosslinked hydrogels, porous scaffolds, hydrolytic stability, cell adhesion, cell proliferation, biocompatibility, tissue reaction, wound healing, bone regeneration, hemostasis, peripheral nerve repair
- MeSH terms
- Animals, Biocompatible Materials, Cell Adhesion, Cell Line, Cell Survival, Electrophoresis, Polyacrylamide Gel, Hair, Humans, Keratins, Male, Microscopy, Electron, Scanning, Models, Biological, Hydrogels, Tissue Engineering, NIH 3T3 Cells, Cell Proliferation, Mice, Tissue Scaffolds
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