Cross-Linked Gamma Polyglutamic Acid/Human Hair Keratin Electrospun Nanofibrous Scaffolds with Excellent Biocompatibility and Biodegradability

Abstract

Recently, human hair keratin has been widely studied and applied in clinical fields due to its good histocompatibility, biocompatibility, and biodegradability. However, the regenerated keratin from human hair cannot be electrospun alone because of its low molecular weight. Herein, gamma polyglutamic acid (γ-PGA) was first selected to fabricate smooth and uniform γ-PGA/keratin composite scaffolds with excellent biocompatibility and biodegradability by electrospinning technology and a chemical cross-linking method in this study. The effect of electrospinning parameters on the structure and morphology, the mechanism of chemical cross-linking, biocompatibility in vitro cell culture experiments, and biodegradability in phosphate-buffered saline buffer solution and trypsin solution of the γ-PGA/keratin electrospun nanofibrous scaffolds (ENS) was studied. The results show that the cross-linked γ-PGA/keratin ENSs had excellent water stability and biodegradability. The γ-PGA/keratin ENSs showed better biocompatibility in promoting cell adhesion and cell growth compared with the γ-PGA ENSs. It is expected that γ-PGA/keratin ENSs will be easily and significantly used in tissue engineering to repair or regenerate materials.

Biocompatibility of KAPs-Depleted Residual Hair

“…6) was thin (with 28% mean) compared to a much thicker reaction in pacemaker implants in the mm range at ~ 100% of the dermis thickness [24]. The paper's objective outcome correlated with numerous previous studies on extracted and reassembled keratins and KAPs or the broad term "keratin biomaterials," with or without other accepted polymeric biomaterials, showing good in vitro and in vivo biocompatibilities [10,12,[33][34][35]. In the absence of the hair follicle which is the antigenic region [36] containing intact living cells, the terminal hair shaft or fiber is a non-immunogenic non-living biomaterial primarily due to its highly-conserved protein molecular structures across species [3,37,38].…”