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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BackgroundKeratin nanofibers in tissue engineering: bridging nature and innovation
Aadil, K. R., Bhange, K., Kumar, N., & Mishra, G. (2024) · Biotechnology for Sustainable Materials · doi:10.1186/s44316-024-00019-6 · Cited by 22
“Similar results have been found by other researchers in which it promoted cell adhesion in NIH-3T3 fibroblast cell adhesion over uncoated dish culture [42].”
Isolation and physicochemical characterization of biopolymers
Jacob, J., & Gopi, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819240-5.00003-1 · Cited by 21
Zuniga, K., Gadde, M., Scheftel, J., Senecal, K. J., Cressman, E. N. K., Dyke, M. E. V., & Rylander, M. N. (2021) · International Journal of Hyperthermia · doi:10.1080/02656736.2021.1930202 · Cited by 23
“Our results indicate a trend in increasing denaturing temperature with greater KTN, in which KTN may act as a secondary crosslinker and stabilize the collagen hydrogels produced with primary crosslinking [60].”
BackgroundResultSilk Fibroin/Wool Keratin Composite Scaffold with Hierarchical Fibrous and Porous Structure
Yang, J., Wang, H., Zhou, Y., Duan, L., Schneider, K. H., Zheng, Z., Han, F., Wang, X., & Li, G. (2023) · Macromolecular Bioscience · doi:10.1002/mabi.202300105 · Cited by 21
EXPERIMENTAL TAPHONOMY OF KERATIN: A STRUCTURAL ANALYSIS OF EARLY TAPHONOMIC CHANGES
Saitta, E. T., Rogers, C. S., Brooker, R. A., & Vinther, J. (2017) · Palaios · doi:10.2110/palo.2017.051 · Cited by 21
In vitro and in vivo Assessment of Keratose as a Novel Excipient of Paclitaxel Coated Balloons
Turner, E. A., Erwin, M. M., Atigh, M. K., Christians, U., Saul, J. M., & Yazdani, S. K. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00808 · Cited by 21
“Keratose, the oxidatively purified extract of keratin, has low toxicity and immunogenicity and can spontaneously forms scaffolds capable of eluting drugs/factors in a concentration-dependent manner (Hill et al., 2010; de Guzman et al., 2011; Saul et al., 2011; Burnett et al., 2013).”
BackgroundEffects of Graphene Oxide on the Structure and Properties of Regenerated Wool Keratin Films
Li, B., Yao, J., Niu, J., Liu, J., Wang, L., Mao, F., & Sun, Y. (2018) · Polymers · doi:10.3390/polym10121318 · Cited by 20
Joo, S., Kim, J. H., Lee, C., Kang, J., Seo, S., Kim, J.-H., & Song, Y. (2022) · ACS Applied Bio Materials · doi:10.1021/acsabm.2c00736 · Cited by 21
Tu, H., Yu, W., & Duan, L. (2016) · Journal of Materials Science · doi:10.1007/s10853-016-0140-0 · Cited by 20
“Wool keratin has been demonstrated as an attractive natural biomaterial for biomedical use in a similar manner to collagen and gelatin [25, 26].”
BackgroundCryogelation of Human Hair Keratins
Chua, H. M., Zhao, Z., & Ng, K. W. (2020) · Macromolecular Rapid Communications · doi:10.1002/marc.202000254 · Cited by 20
Keratose hydrogel for tissue regeneration and drug delivery
Ledford, B. T., Barron, C., Dyke, M. E. V., & He, J. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.06.017 · Cited by 19
Safety Assessment of Keratin and Keratin-Derived Ingredients as Used in Cosmetics
Burnett, C. L., Bergfeld, W. F., Belsito, D. V., Hill, R. A., Klaassen, C. D., Liebler, D. C., Marks, J. G., Shank, R. C., Slaga, T. J., Snyder, P. W., et al. (2021) · International Journal of Toxicology · doi:10.1177/10915818211013019 · Cited by 19
“Keratin proteins extracted from hair are classified into 3 broad groups: a, b, and g.(13) a-Keratin (found in hair fiber cortex) is low in sulfur content and has an average MW of 60 to 80 kDa.”
BackgroundBridging Nature and Engineering: Protein-Derived Materials for Bio-Inspired Applications
Nawaz, T., Gu, L., Gibbons, J., Hu, Z., & Zhou, R. (2024) · Biomimetics · doi:10.3390/biomimetics9060373 · Cited by 19
“The extraction of β -keratins is difficult [195].”
BackgroundPEG-Immobilized Keratin for Protein Drug Sequestration and pH-Mediated Delivery
de Guzman, R. C., & Rabbany, S. Y. (2016) · Journal of Drug Delivery · doi:10.1155/2016/7843951 · Cited by 19
Flores‐Hernandez, C. G., Velasco‐Santos, C., Rivera‐Armenta, J. L., Gómez-Guzmán, O., Yáñez-Limón, J. M., Olivas-Armendáriz, I., López‐Barroso, J., & Martínez‐Hernández, A. L. (2020) · Journal of Applied Polymer Science · doi:10.1002/app.50321 · Cited by 18
Mahajan, N. M., Wanaskar, K., Ali, N., Mahapatra, D. K., Iqbal, M., Bhat, A., & Kaleem, M. (2023) · Gels · doi:10.3390/gels9060462 · Cited by 18
“The protein is hard, resilient, and lighter because the sulphur atoms in the remnants of cysteine frequently interconnect with each other [11].”
BackgroundSingh, V., Wang, S., & Ng, K. W. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803581-8.09317-6 · Cited by 18
Zou, M., Zhou, J., Xu, L., Song, J., Liu, S., & Li, X. (2019) · Micron · doi:10.1016/j.micron.2019.102735 · Cited by 17
Silva, O. A., Pellá, M. C. G., Popat, K. C., Kipper, M. J., Rubira, A. F., Martins, A. F., Follmann, H. D. M., & Silva, R. (2021) · Advanced Powder Technology · doi:10.1016/j.apt.2021.11.005 · Cited by 17
Khumalo, M., Sithole, B. B., Tesfaye, T., & Lekha, P. (2022) · Journal of Nanomaterials · doi:10.1155/2022/7080278 · Cited by 17
Xu, X.-L., Wang, B., Liu, Y., Li, W.-X., Wu, J., Yuan, H., Xu, X., & Chen, D. (2022) · Microchemical Journal · doi:10.1016/j.microc.2022.108274 · Cited by 17
Vasoactive Properties of Keratin-Derived Compounds
Nuñez, F. A., Trach, S., Burnett, L., HANDA, R., Dyke, M. E. V., Callahan, M. F., & Smith, T. L. (2011) · Microcirculation · doi:10.1111/j.1549-8719.2011.00135.x · Cited by 17
pH and thermo-responsive hybrid hydrogels based on PNIPAAM and keratin
do Lago, G. L., & Felisberti, M. I. (2020) · European Polymer Journal · doi:10.1016/j.eurpolymj.2020.109538 · Cited by 17
Hara, K. Y., Kim, S., Yoshida, H., Kiriyama, K., Kondo, T., Okai, N., Ogino, C., Fukuda, H., & Kondo, A. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3665-9 · Cited by 17
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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