Biopolym. Cell. 2021; 37(5):335-345.
http://dx.doi.org/10.7124/bc.000A5F
Structure and Function of Biopolymers
Characteristics of regenerated keratin and keratin-based film
1Havryliak V. V., 2Mykhaliuk V. V., 1Kochubei V. V.
  1. Lviv Polytechnic National University
    12, S. Bandery Str., Lviv, Ukraine, 79013
  2. Institute of Animal Biology, NAAS of Ukraine
    38, Stusa Str., Lviv, Ukraine, 79034

Abstract

Aim. Determination of the characteristics of regenerated keratin obtained from human hair, development of keratin-based films, and study[ing] their surface morphology and adsorption capacity. Methods. Keratins were extracted by sulfitolysis. The structure of regenerated keratin was studied by IR spectroscopy, thermogravimetry, and electrophoresis. Keratin-based films were made by casting. Their biocompatibility was analyzed in the adsorption test by incubation in human serum. Scanning electron microscopy was used to evaluate the surface morphology of the films. Results. The regenerated keratin is represented mainly by proteins of intermediate filaments and is characterized by better thermal properties than the native one. The keratin-based films had a pronounced relief structure. The adsorption test shows the ability of the films to adsorb albumin from human serum on their surface. Conclusions. The mild extraction of keratins by sulfitolysis ensures the preservation of their native properties and the ability of keratin-based films to form bonds with blood proteins.
Keywords: biopolymers, keratin, sulfitolysis, thermogravimetric analysis, films, adsorption
Full text: (PDF, in English)

References

[1] Gupta P, Nayak K. Characteristics of protein-based biopolymer and its application. Polym Eng Sci. 2015; 55(3): 485-98.
[2] Yang Y, Chen J, Migliaresi C, Motta A. Natural fibrous protein for advanced tissue engineering applications: focusing on silk fibroin and keratin. Adv Exp Med Biol. 2020; 1249:39-49.
[3] Makar IA, Gavrylyak V, Sedilo G. Genetical and biochemical aspects of keratin synthesis by hair follicles. Cyt Genet. 2007; 41(1):75-9.
[4] Hassan, Mohammad M, Christopher M. Carr. A review of the sustainable methods in imparting shrink resistance to wool fabrics. J Adv Res. 2019; 18:39-60.
[5] Shuai W, Taraballi F, Lay P, Kee W. Human keratin hydrogels support fibroblast attachment and proliferation in vitro. Cell Tissue Res. 2012; 347:795-802.
[6] Pace L, Plate J, Smith T, Van D. The effect of human hair keratin hydrogel on early cellular response to sciatic nerve injury in a rat model. Biomaterials. 2013; 34(24):5907-14.
[7] Aluigi A, Vineis C, Varesano A, Mazzuchetti G, Ferrero F, Tonin C. Structure and properties of keratin/PEO blend nanofibres. Eur Polym J. 2008; 44(8):2465-75.
[8] Passipieri J, Baker H, Siriwardane M, Ellenburg M, Vadhavkar M, Saul J, Tomblyn S, Burnett L, Christ G. Keratin hydrogel enhances in vivo skeletal muscle function in a rat model of volumetric muscle loss. Tissue Eng Part A. 2017; 23(11-12):556-71.
[9] Borelli M, Joepen N, Reichl S, Finis D, Schoppe M, Geerling G, Schrader S. Keratin films for ocular surface reconstruction: Evaluation of biocompatibilityin an in-vivo model. Biomaterials. 2015; 42:112-120.
[10] Bochynska-Czyz M, Redkiewicz P, Kozlowska H, Matalinska J, Konop M, Kosson P. Can keratin scaffolds be used for creating threedimensional cell cultures? Open Med. 2020; 15:249-53.
[11] Cheng Z, Chen X, Zhai D, Gao F, Guo T, Li W, Wang B. Development of keratin nanoparticles for controlled gastric mucoadhesion and drug release. J Nanobiotechnol. 2018; 16(1):1-13.
[12] Gao F, Li W, Deng J, Kan J, Guo T, Wang B, Hao S. Recombinant human hair keratin nanoparticles accelerate dermal wound healing. ACS Appl Mater Interfaces. 2019; 11(20):18681-90.
[13] Sierpinski P, Garrett J, Ma J, Apel P, Klorig D, Smith T, Van Dyke M. The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves. Biomaterials. 2008; 29(1):118-28.
[14] Havryliak V, Mykhaliuk V, Petrina R, Fedorova O, Lubenets V, Novikov V. Adsorbents based on keratin for lead and cadmium removal. Curr Appl Sci Techno. 2020; 20(1):136-43.
[15] Sadeghi S, Nourmohammadi J, Ghaee A, Soleimani N. Carboxymethyl cellulose-human hair keratin hydrogel with controlled clindamycin release as antibacterial wound dressing. Int J Biol Macromol. 2020; 147:1239-47.
[16] Silva N, Vilela C, Marrucho I, Freire S, Neto C, Silvestre J. Protein-based materials: from sources to innovative sustainable materials for biomedical applications. J Mater Chem B. 2014; 2(24):3715-40.
[17] Saha S, Arshad M, Zubair M, Ullah A. Keratin as a Biopolymer. In Keratin as a Protein Biopolymer Springer, Cham. 2019; 163-85.
[18] Isarankura N, Ayutthaya SIN, Tanpichai S, Wootthikanokkhan J. Keratin extracted from chicken feather waste: extraction, preparation, and structural characterization of the keratin and keratin/biopolymer films and electrospuns. J Polym Environ. 2015; 23(4):506-16.
[19] Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dyebinding. Anal Biochem. 1976; 72:248-54.
[20] Laemmli U. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5.
[21] Rocha Plácido Moore G, Maria Martelli S, Gandolfo C, José do Amaral Sobral P, Borges Laurindo J. Influence of the glycerol concentration on some physical properties of feather keratin films. Food Hydrocoll. 2006; 20(7):975-82.
[22] Shavandi A, Silva T, Bekhit A, Bekhit A. E. Keratin: dissolution, extraction and biomedical application. Biomater Sci. 2017; 5(9): 1699-735.
[23] Roy K, Choi W, Yi W, Moon W, Lee R, Han K, Hasebe T. Hemocompatibility of surface-modified, silicon-incorporated, diamond-like carbon films. Acta Biomater. 2009; 5(1):249-56.
[24] Rajabi M, Ali A, McConnell M, Cabral J. Keratinous materials: Structures and functions in biomedical applications. Mater Sci Eng: C. 2020; 110:110612.
[25] Aziz M. E, Jaleeli K. A, Ahmad A. FTIR spectroscopic analysis of keratinized tissue-the Hair. Int J Sci Eng Technol. 2017; 6:105-7.
[26] de Castro Lima C, Machado L, Velasco M, Du Rosario Matos J. DSC measurements in relation to hair studies. J Therm Anal Calorim. 2018; 132:1429-37.
[27] Apostolidou C. Regenerated hoof keratin from 1-ethyl-3methylimidazolium acetate and insights into disulfide ionic liquid interactions from MD Simulation. Chemistry Open. 2020; 9:695-702.
[28] McLellan J, Thornhill S, Shelton S, Kumar M. Keratin-based biofilms, hydrogels, and biofibers. Keratin as a Protein Biopolymer. Springer Series on Polymer and Composite Materials. Springer, Cham. 2019; 187-200.
[29] Rahmati M, Mozafari M. Protein adsorption on polymers. Mater Today Commun. 2018; 17:527-540.
[30] Vasilchina H, Popov C, Ulrich S, Ye J, Danneil F, Stüber M, Welle A. Wetting behaviour and protein adsorption tests on ultrananocrystalline diamond and amorphous hydrogenated carbon thin films. Nanostructured Materials for Advanced Technological Applications. NATO Science for Peace and Security. Series B: Physics and Biophysics, Dordrecht: Springer. 2009. 547.
[31] Popov C, Vasilchina H, Kulisch W, Danneil F, Stüber M, Ulrich S, Welle A, Reithmaier JP. Wettability and protein adsorption on ultrananocrystalline diamond/amorphous carbon composite films. Diam Relat Mater. 2009; 18:895-8.