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Keratin-based Bioplastic from Chicken Feathers
Published in Abdullah Al-Mamun, Jonathan Y. Chen, Industrial Applications of Biopolymers and their Environmental Impact, 2020
A. Gupta, B.Y. Alashwal, Md. S. Bala, N. Ramakrishnan
In addition, extracted keratins can form self-assembled structures that regulate cellular recognition and behavior. These qualities have led to the development of keratin biomaterials with applications in wound healing, drug delivery, tissue engineering, trauma and medical devices.
Polymer Materials for Oral and Craniofacial Tissue Engineering
Published in Vincenzo Guarino, Marco Antonio Alvarez-Pérez, Current Advances in Oral and Craniofacial Tissue Engineering, 2020
Iriczalli Cruz Maya, Vincenzo Guarino
Keratin is a fibrous protein, found in hair, wool, feathers, nails and horns of mammals, reptiles and birds. Keratin proteins can be classified in intermediate filament proteins and the matrix proteins. The characteristic secondary structure of intermediate filaments is a-helix, also known as α-keratins and are low in sulfur content. The matrix proteins are globular, have high sulfur content and are surrounding the intermediate filament proteins interacting through disulfide bonds (Magin et al. 2007). Keratin is characterized by the presence of sequences as RGD (Arg-Gly-Asp) and LDV (Leu-Asp-Val) found in several ECM proteins for cell adhesion. Thus, keratin has been proposed as an alternative to collagen for developing biomaterials for tissue regeneration (Srinivasan et al. 2010). Besides, several studies have shown that the addition of keratin and adjusting its concentration, improved the mechanical properties of biomaterials (Zhang et al. 2014; Wang et al. 2015).
Proteins for Conditioning Hair and Skin
Published in Randy Schueller, Perry Romanowski, Conditioning Agents for Hair and Skin, 2020
Keratin, as the primary structural protein of hair (and nails as well), provides hair its strength. Keratin hydrolyzates are notable primarily because of their high cystine content (see Tables 2 and 3), which, in a reducing environment, allows for sulfhydryl interchange with cysteine residues in hair. High-molecular-weight hydrolyzed keratin (125,000 Da) demonstrated long-term substantivity and conditioning effects when applied to reduced hair (i.e., in the midst of permanent waving) at a 1.5-5% solids level (27). Patents related to alkaline permanent waving and the better afterfeel which resulted from incorporation of these hydrolyzates were issued in the early 1980s (28,29).
Recent progress in the conversion of biomass wastes into functional materials for value-added applications
Published in Science and Technology of Advanced Materials, 2020
Keratin is a significant component in hair, chicken or bird’s feathers, bristles, horns, hooves, and nails. Millions tonnes of keratin containing wastes are produced every year over the world, typically in poultry slaughterhouses and fabric textile industry [45]. The content of keratin in animal hair (including human hair) and poultry feathers is over 90% [104]. It is present as α-keratin in hair, horns and hoofs and β-keratin in bird feathers, respectively. Keratin plays an important role in providing a tough matrix for substances due to its mechanically durable property. The extraction, purification and characterization of keratin from raw materials can facilitate the development of keratin-based materials for tissue engineering [76], cosmetics, agriculture, and biodegradable packaging [45].
One-step fabricated keratin nanoparticles as pH and redox-responsive drug nanocarriers
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Xuelian Zhi, Pengcheng Liu, Yanmei Li, Pengfei Li, Jiang Yuan, Jiantao Lin
Keratin is an ideal material for versatile drug delivery due to its good biocompatibility, biodegradability, absorbability, and non-immunogenicity [35]. It contains abundant polar side chains made of disulfide, carboxyl and amino groups, endowing keratin with high chemical reactivity. Previously, pH and redox dual responsive keratin based drug-loaded nanoparticles (KDNPs) have been fabricated through two-step strategies in our group [36]. That is, keratin nanoparticles were first prepared by desolvation method, followed by electrostatic adsorbing doxorubicin (DOX) to afford drug loaded keratin nanoparticles (KDNPs). Herein, we purposed to develop a one-step method to fabricate keratin-based drug delivery systems (Figure 1). Keratin/DOX complexes were first prepared by drug induced ionic gelation technique via electrostatic interactions. Then, DOX loaded keratin nanoparticles (KDNPs) were prepared by the desolvation method. To stabilize the formed keratin particles, glutaraldehyde was added for cross-linking. Subsequently, the size, zeta potential, and drug-loading capacity of KDNPs were characterized with DLS, SEM, and UV. The cell toxicity of KDNPs was evaluated with MTT assay. The pH/GSH dependent DOX delivery behaviors of KDNPs were also explored.
Evaluating the antioxidant effects of human hair protein extracts
Published in Journal of Biomaterials Science, Polymer Edition, 2018
Hui Ying Lai, Shuai Wang, Vaishali Singh, Luong T. H. Nguyen, Kee Woei Ng
Keratin is a class of intermediate filament structural proteins that can be found in the epidermis and epidermal appendages of vertebrates such as wool, nails, feathers, hooves, and hair. Together with keratin associated proteins (KAPs), they confer unique mechanical properties found in the epidermal appendages. As biomaterials, these proteins exhibit tremendous potential as regenerative substrates due to their inherent biocompatibility, biodegradability and bioactivity [1–4]. Keratins and KAPs derived from human hair offer several advantages over its animal counterparts due to its potentially lower immunogenicity and the possibility to personalize autologous material platforms depending on the patient’s needs. Abundant and readily available supplies of human hair make this an economical source of human-derived bioactive biomaterials. To this end, keratin-based coatings, films, hydrogels, sponges, and fibers have been explored in various tissue engineering and regenerative medicine applications [5–10].