The DOI matches its Crossref record; 37 of the 42 references it cites were found in a registry or an index.
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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“[13] Human hair *, ** Keratin hydrogel Excellent biocompatibility, peripheral nerve regeneration in rabbits”
BackgroundSaul, J. M., Bohnert, J. S., O’Brien, M., Alnuaimi, S., Carnwath, T. P., Dunivan, Q., Coffin, D. W., & Smith, T. L. (2025) · Tissue Engineering and Regenerative Medicine · doi:10.1007/s13770-025-00747-4 · Cited by 3
“However, keratins extracted from a similar source and by similar methods have previously been characterized by protein-induced X-ray emission for elemental analysis, amino acid analysis, thiol content, SEM for porosity, rheological properties, and mechanical properties [14, 32–34].”
Zafeer, M. K., Raza, S., Junaid, L., & Bhat, K. S. (2025) · Journal of Natural Fibers · doi:10.1080/15440478.2025.2586392 · Cited by 3
“Keratin derived from oxidation is termed keratose, whereas that obtained from reduction is known as kerateines (Hill, Brantley, and Van Dyke 2010; Richter et al. 2012).”
Mondal, M. C., Uddin, H. M. W., Ashrafi, S., Malitha, S. B., Shuvo, S. I., & Saif, T. (2026) · The Protein Journal · doi:10.1007/s10930-026-10346-4 · Cited by 4
Is ancestry, not natron, an explanation for fair haired children in Greco-Roman Egypt?
Davey, J., & Spring, G. (2020) · Forensic Science Medicine and Pathology · doi:10.1007/s12024-020-00225-4 · Cited by 3
Evaluation of Biological Degraded Keratin for Biogas Production Using Dry Anaerobic Digestion System
Setyaningrum, S., Patinvoh, R. J., Purwadi, R., & Taherzadeh, M. J. (2021) · Current Journal International Journal Applied Technology Research · doi:10.35313/ijatr.v2i2.49 · Cited by 3
“Meanwhile β-keratin has a pleated sheet structure and is not elastic (Hill et al., 2010).”
BackgroundElectrospun Nanofibrous Scaffolds for Neural Tissue Engineering
Pramanik, S., & Muthuvijayan, V. (2022) · Advances in polymer science · doi:10.1007/12_2022_130 · Cited by 3
Fitriyanto, N. A., Ramadhanti, Y., Rismiyati, Rusyadi, I., Pertiwiningrum, A., Prasetyo, R. A., & Erwanto, Y. (2022) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/1059/1/012026 · Cited by 3
“[36] stated the characteristic band of protein αkeratin protein around 43 to 64 kDa, which describes acidity.”
BackgroundÇakmak, E. (2023) · Archiv für Geflügelkunde · doi:10.1399/eps.2023.376 · Cited by 3
Samide, A. P., Iacobescu, G. E., Tutunaru, B., Tigae, C., Spînu, C., & Oprea, B. (2024) · Polymers · doi:10.3390/polym16050669 · Cited by 3
Ledford, B. T., Chen, M., Dyke, M. E. V., Barron, C., Zhang, X., Cartaya, A., Zheng, Y., Ceylan, A., Goldstein, A. S., & He, J. (2023) · Stem Cell Reviews and Reports · doi:10.1007/s12015-023-10574-6 · Cited by 3
Keratin as Renewable Material to Develop Polymer Composites: Natural and Synthetic Matrices
Flores‐Hernandez, C. G., Murillo-Segovia, B., Martínez‐Hernández, A. L., & Velasco‐Santos, C. (2017) · Handbook of Composites from Renewable Materials · doi:10.1002/9781119441632.ch105 · Cited by 3
Fabrication of feather keratin bio-based materials: Thermoplastics and tissue engineered scaffolds
Esparza, Y. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r39w09c65 · Cited by 4
Bioproteins: Fabrication and Application
Khan, M. N., Islam, T., Alam, M. A., & Khan, R. A. (2016) · Taylor & Francis eBooks · doi:10.1081/e-ebpp-120049962 · Cited by 3
Animal-Derived Biopolymers: Properties, Raw Material Sources, and Their Developmental Process
Hossain, Z. M. (2026) · Materials horizons · doi:10.1007/978-981-95-2258-3_2 · Cited by 2
Lokeshwari, B., Saranraj, P., Al-Abedi, H. F. H., Al-Abedi, S. F. H., Al-Magsoosi, H. H. E., Jaafar, M. T., Essa, I. M., Gharban, H. A. J., Gayathri, K., & Cardoso, A. M. (2026) · Resources · doi:10.3390/resources15030046 · Cited by 2
Production and characterisation of mucilage-based keratin films using goose feathers
Ünver, E., & Çakmak, E. (2023) · Archiv für Geflügelkunde · doi:10.1399/eps.2023.381 · Cited by 2
Polymers in tissue engineering and regenerative medicine
Ezzati, N., Asadi, E., Azodi‐Deilami, S., & Saber‐Samandari, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823797-7.00017-4 · Cited by 2
Keratin Hydrolysate from Wool By-products as an Additive for Dyeing Bovine Leathers
Berechet, M. D., Gaidau, C. C., Simion, D., & Șendrea, C. (2023) · Leather and Footwear Journal · doi:10.24264/lfj.23.3.1 · Cited by 2
Sustainable Cationic Cotton with Keratin Hydrolysate
Bulut, M. O., & Akçalı, K. (2024) · Fibers and Polymers · doi:10.1007/s12221-024-00626-0 · Cited by 2
In Vitro Characterization of Scaffolds for Tissue Engineering - A Review
Baliga, A., & Borkar, S. (2016) · International Journal of Advanced Engineering Research and Science · doi:10.22161/ijaers/3.10.33 · Cited by 2
Study on Obtaining Keratin Extracts from Leather Industry By-products
Niculescu, M. D., Berechet, M. D., Gaidau, C. C., Ignat, M., & Radu, M. (2016) · ICAMS · doi:10.24264/icams-2016.iv.7 · Cited by 2
“The bands at 600-700 cm-1 attributed to stretching vibration νC-S and at 800-900 cm-1 attributed to rocking vibration δS-H are specific to sulfur compounds (Khosa and Ullah, 2014; Hill et al., 2010; Staron et al., 2014).”
BackgroundMethodRegenerated Sustainable Fibres
Lakshmanan, S. O., & Raghavendran, G. (2018) · Textile science and clothing technology · doi:10.1007/978-981-10-8578-9_2 · Cited by 2
Preparation of human hair keratin/calcium alginate blend films
Zhang, L., Wang, Q., Lin, C. B., Wang, Q. Q., Sui, S. Y., & Zhu, P. (2019) · Ferroelectrics · doi:10.1080/00150193.2019.1592480 · Cited by 1
Improvement of Flexibility of Keratin Film by Zinc Acetate
Srihanam, P., & Srisuwan, Y. (2020) · Materials science forum · doi:10.4028/www.scientific.net/msf.1003.191 · Cited by 1
“This region is a response for cysteic acid which is derived from cysteine degradation in keratin [18].”
Background
Metadata
- 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
- Physical Sciences › Materials Science › Biomaterials › 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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