...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>RSC Advances >Sustained release of nerve growth factor from highly homogenous cubosomes stabilized by beta-casein with enhanced bioactivity and bioavailability
【24h】

Sustained release of nerve growth factor from highly homogenous cubosomes stabilized by beta-casein with enhanced bioactivity and bioavailability

机译：从β-酪蛋白稳定的高度均匀缔约置的神经生长因子持续释放，具有增强的生物活性和生物利用度

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Controlling the specific ionic interactions between drugs and mesophases particles can enable controlled release systems for proteins. Here we present the interaction of basic nerve growth factor (NGF) with highly homogeneous cubosomes based on the glycerol monooleate-water system where beta-casein was employed as a stabilizer. Addition of beta-casein leads to modification of the internal cubosomal surface to generate highly negative charge. The colloidal structures were characterized with small angle X-ray scattering and visualized using cryogenic transmission electron microscopy. These nanostructured particles are able to sustain the release of hydrophilic NGF since less than 15% of the protein was released over 24 h. Similarly, cationic 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP) immobilized within the mesophase particles provided another specific interactions of the cubosomal surface, from which the release of water soluble bovine serum albumin was retarded. Evaluation of NGF entrapped colloidal dispersions in PC12 cells led to identification of beta-casein stabilized cubosomes that induce more than 140% neurite outgrowth enhancing the activity of NGF. Accordingly, the AUC value for RWM administration of NGF-loaded dispersions in guinea pigs was significantly higher than that administrated with NGF, of which the relative bioavailability of the beta-casein stabilized dispersions was increased to 337% as compared with free drug.
机译：控制药物和中间蛋白酶颗粒之间的特定离子相互作用可以使蛋白质的控制释放系统能够实现。在这里，我们呈现基于甘油单烯酸盐水系统的高度均匀立方体的基础神经生长因子（NGF）的相互作用，其中β-酪蛋白作为稳定剂。添加β-酪蛋白导致内部立方体表面的改性以产生高负电荷。胶体结构中还存在小角度X射线散射和使用低温透射电子显微镜观察。这些纳米结构颗粒能够维持亲水性NGF的释放，因为少于15％的蛋白质释放超过24小时。类似地，固定在中间相颗粒内的阳离子1,2-二牛-3-三甲基三甲基丙烷 - 丙烷（DOTAP）提供了立方体表面的另一个特异性相互作用，从中延迟了水溶性牛血清白蛋白的释放。 PC12细胞中NGF捕获的胶体分散体的评估导致β-酪蛋白稳定的缔约肌诱导的诱导超过140％的神经沸石过度增强NGF的活性。因此，RWM施用NGF负载的豚鼠的分散体的AUC值显着高于NGF，其中β-酪蛋白稳定的分散体的相对生物利用度与游离药物相比增加至337％。

著录项

  • 来源
    《RSC Advances》 |2016年第115期|共9页
  • 作者

    Che Xin; Wang Zhenjie; Liu Yining; Sun Yanhui; Liu Hongzhuo;

  • 作者单位

    Shenyang Pharmaceut Univ Sch Pharm 103 Wenhua Rd Shenyang 110016 Peoples R China;

    Shenyang Pharmaceut Univ Sch Pharm 103 Wenhua Rd Shenyang 110016 Peoples R China;

    Shenyang Pharmaceut Univ Sch Pharm 103 Wenhua Rd Shenyang 110016 Peoples R China;

    Shenyang Pharmaceut Univ Sch Pharm 103 Wenhua Rd Shenyang 110016 Peoples R China;

    Shenyang Pharmaceut Univ Sch Pharm 103 Wenhua Rd Shenyang 110016 Peoples R China;

  • 收录信息
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

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