Fabrication of thin transparent collagen film using collagen extract from pig skin

摘要

Introduction: Collagen is one of the most studied and used biomolecules in tissue engineering because of its high biocompatibility, biodegradability, and low antigenicity. However, its wide application in tissue engineering is limited since collagen is obtained through a quite complicated extraction process and exhibits poor mechanical and enzymatic resistance. In this study, we extracted type Ⅰ collagen from pig skin and produced thin transparent collagen film after crosslinking. Materials and Methods: Type Ⅰ atelocollagen was extracted from pig skin using acetic acid in the presence of pepsin, and then purified by dialysis against distilled water and lyophilized. The collagen purity was assessed by SDS-PAGE and collagen assay kit. Extracted collagen was crosslinked using 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimied (EDC) with N-hydroxysuccinimide (NHS). Thin transparent collagen film was produced by air-drying of crosslinked or non-crosslinked collagen solution. Results and Discussion: The extracted collagen contained two a-chains and one β-chain, and the purity was similar to that of the FDA approved collagen (Atelocollagen, Tissen, Republic of Korea). Both thin collagen film fabricated from crosslinked or non-crosslinked collagen were durable and transparent. Moreover, their characteristics were maintained well even in PBS for 7 days. Conclusions: We could set up a simple but effective collagen extraction procedure from pig skin. Additionally, we fabricated thin transparent collagen film and evaluated its stability. While more studies are required, this study will allow the next steps in the development of a corneal bandage and a tissue-engineered cornea.