...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Environmental Science & Technology >Interaction forces between colloids and protein-coated surfaces measured using an atomic force microscope
【24h】

Interaction forces between colloids and protein-coated surfaces measured using an atomic force microscope

机译：使用原子力显微镜测量胶体和蛋白涂层表面之间的相互作用力

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Bacterial surfaces contain proteins, polysaccharides, and other biopolymers that can affect their adhesion to another surface. To better understand the role of proteins in bacterial adhesion, the interactions between two different model colloids (glass beads and carboxylated latex microspheres) and four proteins covalently bonded to glass surfaces were examined using colloid probes and an atomic force microscope (AFM). Adhesion forces between an uncoated glass colloid probe and protein-coated surfaces, measured in retraction force curves, decreased in the order poly-D-lysine > lysozyme > protein A > BSA. This ordering was consistent with the relative calculated charges of the proteins at neutral pH and the zeta-potentials measured for glass beads and latex microspheres coated with these proteins. When the glass bead was coated with a protein (BSA), overall adhesion forces between the protein-coated colloid and the protein-coated surfaces were reduced, and the adhesion force for each protein decreased in the same order observed in experiments with the uncoated glass bead. When latex colloid probes were coated with BSA, adhesion forces were significantly larger than those measured with BSA-coated glass colloid probes under the same conditions, demonstrating that the nature of the underlying colloid can affect the measured interaction forces. In addition, the adhesion forces measured with the BSA-coated latex colloid increased in a different order (BSA :5 lysozyme < protein A < poly-D-lysine) than that observed using the BSA-coated glass colloid. It was also found that increasing the solution ionic strength consistently decreased adhesion forces. This result is contrary to the general observation that bacterial adhesion increases with ionic strength. It was speculated that conformational changes of the protein produced this decrease in adhesion with increased ionic strength. These results suggest the need to measure nanoscale adhesion forces in order to understand better molecular scale interactions between colloids and surfaces.
机译：细菌表面含有蛋白质，多糖和其他生物聚合物，它们可能会影响它们与另一表面的粘附。为了更好地理解蛋白质在细菌粘附中的作用，使用胶体探针和原子力显微镜（AFM）检查了两种不同的模型胶体（玻璃珠和羧化乳胶微球）与共价结合到玻璃表面的四种蛋白质之间的相互作用。用回缩力曲线测得，未包被的玻璃胶体探针与蛋白包被的表面之间的粘附力按聚D-赖氨酸>溶菌酶>蛋白A> BSA的顺序降低。该顺序与蛋白质在中性pH值下的相对计算电荷以及用这些蛋白质包被的玻璃珠和胶乳微球所测得的Zeta电位一致。当玻璃珠上涂有蛋白质（BSA）时，涂有蛋白质的胶体与涂有蛋白质的表面之间的总体粘附力会降低，并且每种蛋白质的粘附力会以未覆盖玻璃的实验中观察到的相同顺序降低珠子。当乳胶胶体探针涂有BSA时，在相同条件下的粘附力明显大于用BSA覆膜的玻璃胶体探针测得的粘附力，这表明底层胶体的性质会影响所测得的相互作用力。此外，与使用BSA涂层的玻璃胶体相比，用BSA涂层的胶乳胶体测量的粘附力以不同的顺序增加（BSA：5溶菌酶<蛋白质A <聚D-赖氨酸）。还发现增加溶液的离子强度始终降低粘附力。该结果与细菌粘附随离子强度增加的一般观察相反。据推测，蛋白质的构象变化导致粘附力降低，离子强度增加。这些结果表明需要测量纳米尺度的粘附力，以了解胶体与表面之间更好的分子尺度相互作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号