Abstract
The aim of this study is to investigate the physicochemical properties, biosafety, and biocompatibility of the collagen extract from the skin of Nile tilapia, and evaluate its use as a potential material for biomedical applications. Two extraction methods were used to obtain acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) from tilapia skin. Amino acid composition, FTIR, and SDS-PAGE results showed that ASC and PSC were type I collagen. The molecular form of ASC and PSC is (α1)2α2. The FTIR spectra of ASC and PSC were similar, and the characteristic peaks corresponding to amide A, amide B, amide I, amide II, and amide III were 3323 cm−1, 2931 cm−1, 1677 cm−1, 1546 cm−1, and 1242 cm−1, respectively. Denaturation temperatures (Td) were 36.1 °C and 34.4 °C, respectively. SEM images showed the loose and porous structure of collagen, indicting its physical foundation for use in applications of biomedical materials. Negative results were obtained in an endotoxin test. Proliferation rates of osteoblastic (MC3T3E1) cells and fibroblast (L929) cells from mouse and human umbilical vein endothelial cells (HUVEC) were increased in the collagen-treated group compared with the controls. Furthermore, the acute systemic toxicity test showed no acute systemic toxicity of the ASC and PSC collagen sponges. These findings indicated that the collagen from Nile tilapia skin is highly biocompatible in nature and could be used as a suitable biomedical material.
Highlights
Collagen is the main structural protein in the extracellular matrix (ECM), constituting approximately 30% of the whole body protein content in animals [1]
The yield of acid-soluble collagen (ASC) was a little bit lower than the yield of pepsin-soluble collagen (PSC), this might be due to the disadvantage of the solubility of cross-links formed through the reaction of aldehyde with lysine and hydroxylysine at telopeptide helical sites [49], which can be explained by the results of Fourier transform infrared (FTIR) analysis
The results showed that ASC and PSC collagen sponges were produced by our process without acute systemic toxicity, and there was not a significant difference from the acute toxicity from commercially available porcine collagen products
Summary
Collagen is the main structural protein in the extracellular matrix (ECM), constituting approximately 30% of the whole body protein content in animals [1]. More than 29 different types of collagen have been identified and described. Most of the collagen is type I [2]. The collagen protein contains triple-helix structures that consist of three almost identical polypeptide chains [3]. Type I collagen is present in bone, skin, dentin, cornea, blood vessels, fibrocartilage, and tendon; it has the unique ability to form fibrils that have high tensile strength and important functions [4,5]. It has been widely used in food manufacturing and the cosmetics industry [6]
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