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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Keratin biomaterials augment anti-inflammatory macrophage phenotype in vitro
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“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
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
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
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
Tran, C. D., Prosenc, F., Franko, M., & Benzi, G. (2016) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2016.06.021 · Cited by 66
“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
“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
“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
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
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
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
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
“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
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 64
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
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
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
“[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
“, 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
“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
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
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 57
“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.”
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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