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.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Citations
Cites
Ellman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824
Foreign body reaction to biomaterials
Anderson, J. M., Rodriguez, A., & Chang, D. T. (2008) · Seminars in Immunology · doi:10.1016/j.smim.2007.11.004 · Cited by 5,138
The secret life of the hair follicle
Hardy, M. H. (1992) · Trends in Genetics · doi:10.1016/0168-9525(92)90350-d · Cited by 931
Jones, C. M., Lyons, K. M., & Hogan, B. L. M. (1991) · Development · doi:10.1242/dev.111.2.531 · Cited by 652
Lyons, K. M., Pelton, R. W., & Hogan, B. L. M. (1990) · Development · doi:10.1242/dev.109.4.833 · Cited by 618
Hill, P. S., Garrett, J. P., Ma, J., Apel, P. J., Klorig, D. C., Smith, T. L., Koman, L. A., Atala, A., & Dyke, M. E. V. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.08.023 · Cited by 346
Self-citationPreparation and characterization of keratin–chitosan composite film
Tanabe, T., Okitsu, N., Tachibana, A., & Yamauchi, K. (2002) · Biomaterials · doi:10.1016/s0142-9612(01)00187-9 · Cited by 318
Crewther, W. G., Fraser, R., Lennox, F. G., & Lindley, H. (1965) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60390-3 · Cited by 306
Fabrication of wool keratin sponge scaffolds for long-term cell cultivation
Tachibana, A., Furuta, Y., Takeshima, H., Tanabe, T., & Yamauchi, K. (2002) · Journal of Biotechnology · doi:10.1016/s0168-1656(01)00395-9 · Cited by 306
Study on the structure and properties of wool keratin regenerated from formic acid
Aluigi, A., Zoccola, M., Vineis, C., Tonin, C., Ferrero, F., & Canetti, M. (2007) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2007.03.002 · Cited by 266
Research works printed but not linked: 8
- Breinl, 1907, The oxidative breaking up of keratin through treatment with hydrogen peroxide, Z Physiol Chem, 52, 158
- Kawano, 1975, Film and gel of keratins, Kagaku To Seibutsu, 13, 291
- Okamoto, 1977, Formation of films from some proteins, Nippon Shokuhin Kogyo Gakkaishi, 24, 40, 10.3136/nskkk1962.24.40 · DOI
- Noishiki, 1982, Application of denatured wool keratin derivatives to an antithrombogenic biomaterial: vascular graft coated with a heparinized keratin derivative, Kobunshi Ronbunshu, 39, 221, 10.1295/koron.39.221 · DOI
- Van Dyke, 2002, Elastomeric biomaterials from human hair keratins as bioactive wound dressings, Abst Papers Amer Chem Soc, 224, U36
- Ito, 1982, Biocompatibility of denatured wool keratin, Kobunshi Ronbunshu, 39, 249, 10.1295/koron.39.249 · DOI
- Valherie I, Gagnieu C. Chemical modifications of keratins: preparation of biomaterials and study of their physical, physiochemical and biological properties. Doctoral thesis. Inst Natl Sci Appl Lyon, France; 1992.
- van de Löcht, 1987, Reconstitution of microfibrils from wool and filaments from epidermis proteins, Melliand Textilberichte, 10, 780
Cited by
Sorted by citations
Items 301–347 of 347
Creation of High-impact-resistant Bioresin from Wool Fabric and its Reversible Resinification
Akioka, S., Hirai, S., Ise, T., Nakayama, D., & Alharbi, M. A. H. (2021) · Fibers and Polymers · doi:10.1007/s12221-021-0415-1 · Cited by 1
Assefa, T., Aremanda, R. B., & Femi, O. E. (2025) · Acta periodica technologica · doi:10.2298/apt250317010a · Cited by 1
Amajuoyi, J. N., Ifegwu, O. C., Ubani-Ukoma, U. N., Okwuba, B. C., Azubuike, C. P., Adeosun, S. O., Lopez, R. F. V., Martin, B. A., & Ilomuanya, M. O. (2026) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2026.104221 · Cited by 1
Extraction of Keratin from Waste Hair Samples for Biotechnological Applications
Ece, E., & Ünlüer, Ö. B. (2026) · Hacettepe Journal of Biology and Chemistry · doi:10.15671/hjbc.1784528 · Cited by 1
Preparation and Characterization of Regenerated Wool Protein PAN Blended Fibers
Ju, W., Liu, H., Xu, S. J., Zheng, L., & Du, B. (2013) · Advanced materials research · doi:10.4028/www.scientific.net/amr.690-693.1461 · Cited by 1
Wongnarat, C., & Srihanam, P. (2020) · Particulate Science And Technology · doi:10.1080/02726351.2020.1789904 · Cited by 1
Extraction of Keratins from Human Hair at Low Pressure and their Characterization
Chaliewsak, J., & Charuchinda, S. (2013) · Advanced materials research · doi:10.4028/www.scientific.net/amr.747.694 · Cited by 1
Siyum, S. (2014) · EngagedScholarship @ Cleveland State University (Cleveland State University) · Cited by 1
Thermoplastic polymer/wool composites
Tanjung, F. A., & Zulkepli, N. N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-824056-4.00018-2 · Cited by 1
Palacio, J. M. O., & Zaritzky, N. (2023) · Ciencia y Tecnología Agropecuaria · doi:10.21930/rcta.vol24_num1_art:2830 · Cited by 1
“Las esponjas de queratina obtenidas de cabello y lana han demostrado buena compatibilidad para aplicaciones en ingeniería de tejidos (Tachibana et al., 2002; Aboushwareb et al., 2009; Hill et al., 2010).”
Lai, H. Y. (2020) · doi:10.32657/10356/146707 · Cited by 1
Hall, R. C. (2014) · OhioLink ETD Center (Ohio Library and Information Network)
Aggregation Behavior of Keratin Proteins Determined by Dynamic Light Scattering
Egert, A. M. (2015) · VTechWorks (Virginia Tech)
Keratose as a Novel Drug Carrier for Drug Coated Balloons
Turner, E. A., Burnett, L., & Yazdani, S. K. (2016) · Southern Biomedical Engineering Conference (SBEC) · doi:10.1109/sbec.2016.33
Bioprocessing of Beef and Pork Meat Processing Industries, ‘Waste to Value‐Add’
Dhakal, D., Shrestha, S. M., & Anal, A. K. (2017) · doi:10.1002/9781118432921.ch17
Bio-based nanocomposites from poultry feather keratin
Kaur, M. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3hh6ck7h
Ledford, B. T. (2018) · VTechWorks (Virginia Tech)
Films and biocomposites based on agro-industrial wastes and by-products
Díaz, T. G. (2019) · Communities in ADDI (University of the Basque Country)
Rapunzel! Rapunzel! How Strong Is Your Hair?
Cranford, S. W. (2020) · Matter · doi:10.1016/j.matt.2019.12.016
Keratin/Egg White Blend Particles: Preparation and Characterization
Tanisood, S., & Srihanam, P. (2020) · Materials science forum · doi:10.4028/www.scientific.net/msf.1003.179
“This peak is a response for cysteic acid which is derived from cystein degradation in keratin [22].”
BackgroundEhrlich, H. (2014) · Biologically-inspired systems · doi:10.1007/978-94-007-5730-1_11
Moffitt, K. (2021) · Queensland University of Technology · doi:10.5204/thesis.eprints.207235
Extraction and Formulation of hydrolyzed-wool keratin solution for hair growth
Abdalraouf, K. A., Elamin, E. S., & Gadien, L. A. (2022) · Omdurman Journal of Pharmaceutical Sciences · doi:10.52981/ojps.v2i3.2876
“During hydrolysis, chemicals break both types of disulfide and peptide bonds in proteins, and as a result the structure of keratin hydrolysate is changed [22] Wool solubilization occurs by disruption of the complex keratin structure.”
BackgroundHorwood, A., & Chockalingam, N. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-85212-8.00003-1 · Cited by 1
Understanding enzyme-mediated keratin hydrolysis and evaluation of new keratin binding peptides
Martinez, J. P. D. O. (2023) · Queensland University of Technology · doi:10.5204/thesis.eprints.239502
Evaluation of keratin templates on dermal regeneration of full-thickness burns
Moay, Z. K. (2023) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/173851
Kuwano, A., Ueno, T., Katsurashima, Y., Tateno, O., & Saitoh, S. (2024) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2024.06.002
Lawrance, A., Devasahayam, L. R. M., Felicita, A. E. S., & Arockianathan, P. M. (2024) · Asian Journal of Chemistry · doi:10.14233/ajchem.2024.31728
Miller, A., Beck, J. P., White, A., Agarwal, J. P., Bachus, K. N., Jeyapalina, S., & Dyke, M. E. V. (2025) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.35551
Strategies to Replace and Regenerate the Cornea and Other Tissues in the Anterior Segment
Bostan, C., Alarcon, E. I., Hanafimosalman, M., Tebid, C. T., Abu‐Dieh, A., Bedford, P., Chandra, A., Dartt, D. A., Davé, V. P., Brunette, I., et al. (2025) · Royal Society of Chemistry eBooks · doi:10.1039/9781839169779-00190
Strnad, S., Žnidarič, M., Škerget, M., Čolnik, M., Gradišnik, L., Maver, U., & Zemljič, L. F. (2025) · ACS Applied Polymer Materials · doi:10.1021/acsapm.5c03027
Keratins’ Advantages and Applications in Tissue Engineering: A Review
Liu, Y.-N., Wang, X., & Yu, P. (2026) · Tissue Engineering Part B Reviews · doi:10.1177/19373368261419661
Challenges and perspectives of natural composites for biomedical applications
Martínez-Álvarez, I. A., Hernández, F., VÁZQUEZ-ELORZA, A., Peresin, M. S., Ortega-Sánchez, C., Godínez, J. B., & García-Carvajal, Z. Y. (2026) · Elsevier eBooks · doi:10.1016/b978-0-323-95754-0.00016-x
Harnessing procoagulation of polymeric hemostats: from molecular design to hemostatic properties
Lu, Y., Yu, H., Wang, L., Meng, Y., Hu, J., & Feng, J. (2026) · Progress in Materials Science · doi:10.1016/j.pmatsci.2026.101747
Sawada, K., & Fujisato, T. (2026) · Journal of Biomaterials Applications · doi:10.1177/08853282261460783
Reduced Keratin For Biomedical Applications
Rijal, M. S., Yee, M. Z. L., Puspitasari, D., Setyawati, M. I., Wibowo, A., Asri, L. A. T. W., & Ng, K. W. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-30151-3.00011-5
Bioactive silver nanocomposite microbeads for advanced wound healing
Turna, E., Baran, N. Y., & Çakmak, E. (2026) · Journal of the Australian Ceramic Society · doi:10.1007/s41779-026-01441-x
Ramesh, P. A., Thangadurai, M., Sethuraman, S., & Subramanian, A. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154521
Ramalingum, N., Bhagwat, P. K., & Pillai, S. (2026) · Biomass Conversion and Biorefinery · doi:10.1007/s13399-026-07276-7
“The process proceeds with a rapid return to atmospheric pressure, resulting in an explosive decompression that triggers the rupture of keratin biomass structural integrity [31].”
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
