【摘要】 用原子力显微镜(AFM)考察了样品质量浓度、溶液pH及温度对鱼鳞胶原蛋白溶液聚集态的影响。结果表明,在pH2.7的醋酸溶液中,当鱼鳞胶原蛋白质量浓度为10μg/mL时,鱼鳞胶原蛋白主要以单体和线性小聚集体形式存在,随着质量浓度继续增大,胶原分子开始自组装形成网状结构,当质量浓度达到4 mg/mL时,形成无规线团结构;而在pH7.2的Tris-HC l溶液中,即使在10μg/mL的低质量浓度下,鱼鳞胶原蛋白也能自组装成不规则的片状聚集体,并通过横向融合形成多孔网状结构。随着质量浓度的增大,纤维直径和高度明显增加;鱼鳞胶原蛋白在40℃处理1 h,其聚集行为发生明显改变,聚集体由线性变为球状;当处理温度升至80℃时,其高级结构基本被破坏,AFM图像上只可见少许不规则分布的团状聚集体。更多还原

【Abstract】 The aggregation behaviors of fish scale collagen at different concentration,temperature and pH were studied by AFM.The results showed that in acidic solution of pH 2.7,collagen existed as fibrillar monomers and linear aggregates were simultaneously observed at low concentration of 10 μg/mL.Collagen self-assembled to network with the increase of concentration,and random coils structure was formed at the concentration of 4 mg/mL.In Tris-HCl solution of pH 7.2,collagen could self-assemble to network structure even at low concentration of 10 μg/mL,and the fibril diameter and height increased evidently with the increase of concentration.The aggregation behaviors changed obviously from linear fibrils to globular aggregates after treated for 1 h at 40 ℃,and the higher-order structure of collagen was almost destroyed by heating for 1 h at 80 ℃,so that only a few anomalistic aggregates could be seen in AFM images.更多还原