Abstract
The aim of the present study was to compare the acute and cumulative cytotoxicity of intact (n-GE) and warmed genipin (w-GE), while investigating the differences in crosslinking capabilities of these two genipins by rheological and mechanical tests. The n-GE solution was prepared by dissolving genipin powder in a sodium phosphate buffer solution. The w-GE solution was prepared by warming the n-GE solution at 37 °C for 24 h. The mechanical tests for chitosan (CH)/genipin gels showed the crosslinking rate of w-GE was much greater than that of n-GE up until 6 h after preparation, whereas the degree of crosslinking of CH/n-GE gels became higher at 12 h. The ISO 10993-5 standard method, which is established specifically for evaluating cumulative cytotoxicity, determined equivalent IC50 for w-GE (0.173 mM) and n-GE (0.166 mM). On the other hand, custom-made cytotoxicity tests using a WST-8 assay after 1 h of cultivation showed that the acute cytotoxicity of w-GE was significantly higher than that of n-GE at concentrations between 0.1–5 mM. The acute cytotoxicity of w-GE should be taken into consideration in its practical uses, despite the fact that the much faster crosslinking of w-GE is useful as an effective cross linker for in-situ forming gels.
Highlights
The mechanical properties and biological stabilities of biopolymers are generally lower than those of synthetic polymers, such as polyesters
The sharpest increases in G was observed for the solution containing 5 mM of warmed genipin (w-GE) immediately after the measurement initiated (Figure 1A)
The fastest gelation rate was observed in w-GE (5 mM), followed by w-GE (2.5 mM), and w-GE (1 mM), which was roughly equivalent to n-GE (5 mM)
Summary
The mechanical properties and biological stabilities of biopolymers (proteins and polysaccharides) are generally lower than those of synthetic polymers, such as polyesters. Various chemical cross linkers have been used for crosslinking biopolymers in tissue fixation [1]. The genipin molecule reacts to a pair of free amine residues on proteins or polysaccharides [13], resulting in crosslinking between them, in which ring-opening polymerization of genipin could be included [14,15]. This reaction between a pair of free amine residues is similar to that of GA; one of the most conventional and effective protein cross linkers
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