Transglutaminase‐modified wool keratin film and its potential application in tissue engineering

Abstract

Transglutaminase (TGase) catalyzes the cross‐linking of many proteins and has been widely used to improve the properties of certain protein‐based materials. Keratin is considered as a promising biomaterial candidate following traditional chemical modification. In this study, the effect of TGase on the properties of a wool keratin film was investigated. The TGase‐modified film was applied to drug release and cell proliferation. Treatment with TGase (30 U/g keratin) for 18 h at 40°C increased the tensile strength of the film from 5.18 ± 0.15 MPa to 6.22 ± 0.11 MPa and decreased the elongation at break from 83.47 ± 1.79% to 72.12 ± 3.02%. The stability of the film in PBS and in artificial gastric juice was also improved. A rougher surface and a more compact cross‐section were observed by scanning electron microscopy photographs of the TGase‐treated film. SDS‐PAGE analysis confirmed that higher molecular weight proteins were formed in the TGase‐modified keratin solution and film. The results of the drug release assay using diclofenac indicated that both films with and without TGase treatment led to a high initial release in PBS, which was more constant in artificial gastric juice. The enzyme treatment led to a lower drug release rate from the film. Cell culture experiments suggested that the TGase‐mediated cross‐linked keratin film shows a good biocompatibility and that it can be used for tissue engineering applications.

Synthesis, structure and antimicrobial property of green composites from cellulose, wool, hair and chicken feather

“…Of particular interest are hairs and chicken feathers as these materials are an important waste product from the salons and poultry industry but are generally left untreated because they have limited solubility and cannot be easily and economically converted to environmentally benign products (Verma et al, 2008; Vilaplana et al, 2010). Keratins are known to possess advantages for wound care, tissue reconstruction, cell seeding and diffusion, and drug delivery as topical or implantable biomaterial (Cui et al, 2013; Hill et al, 2010; Justin et al 2011; Vasconcelos et al, 2013). As implantable film, sheet, or scaffold, keratins can be absorbed by surrounding tissue to provide structural integrity within the body while maintaining stability under mechanical load, and in time can break down to leave neo-tissue (Cui et al, 2013; Hill et al, 2010; Justin et al 2011; Vasconcelos et al, 2013; Verma et al, 2008).…”

One-Pot Synthesis of Biocompatible Silver Nanoparticle Composites from Cellulose and Keratin: Characterization and Antimicrobial Activity

“…[19][20][21][22][23][24][25][26][27][28] KER possesses amino acid sequences similar to those found on an extracellular matrix (ECM), and because ECM is known to interact with integrins, which enable it to support cellular attachment, proliferation, and migration, KER-based materials are expected to have such properties as well. [19][20][21][22][23][24][25][26][27][28] Furthermore, KER is known to possess advantages for wound care, tissue reconstruction, cell seeding and diffusion, and drug delivery.…”

“…[19][20][21][22][23][24][25][26][27][28] KER possesses amino acid sequences similar to those found on an extracellular matrix (ECM), and because ECM is known to interact with integrins, which enable it to support cellular attachment, proliferation, and migration, KER-based materials are expected to have such properties as well. [19][20][21][22][23][24][25][26][27][28] Furthermore, KER is known to possess advantages for wound care, tissue reconstruction, cell seeding and diffusion, and drug delivery. [11][12][13][14][15][16][17][18][19][20] Unfortunately, in spite of its unique properties, KER has relatively poor mechanical properties, and as a consequence, it was not possible to fully exploit the unique properties of KER for various applications.…”

“…[11][12][13][14][15][16][17][18][19][20] Unfortunately, in spite of its unique properties, KER has relatively poor mechanical properties, and as a consequence, it was not possible to fully exploit the unique properties of KER for various applications. [19][20][21][22][23][24][25][26][27][28] To increase the structural strength of KER-based materials, attempts have been made to cross-link KER chains with a cross-linking agent or introduce functional groups to its amino acid residues via chemical reaction(s). [19][20][21][22][23][24][25][26][27][28] The rather complicated, costly, and multistep process is not desirable because it may inadvertently alter its unique properties, making the KER-based materials less biocompatible and toxic and removing or lessening its unique properties.…”

“…[19][20][21][22][23][24][25][26][27][28] To increase the structural strength of KER-based materials, attempts have been made to cross-link KER chains with a cross-linking agent or introduce functional groups to its amino acid residues via chemical reaction(s). [19][20][21][22][23][24][25][26][27][28] The rather complicated, costly, and multistep process is not desirable because it may inadvertently alter its unique properties, making the KER-based materials less biocompatible and toxic and removing or lessening its unique properties. A new method that can improve the structural strength of KER-based products not by synthetic methods but rather by the use of naturally occurring polysaccharides such as CEL is particularly needed.…”