超分子纳米卷的葡萄糖触发的凝与葡萄糖结合的图案
Sihan Yu1, Zhou Ye1, Rajdip Roy1
1Department of Chemical & Biomolecular Engineering, University of Notre Dame, 105 McCourtney Hall, Notre Dame, IN 46556, USA.
Advanced materials (Deerfield Beach, Fla.)
|December 14, 2023
概括
研究人员开发了对葡萄糖敏感的纳米线圈,形成水凝. 这些纳米线圈封装并释放葡萄糖作为对血糖水平的反应,为低血糖症提供了一种新的治疗方法.
科学领域:
- 生物材料科学 生物材料科学
- 纳米技术 纳米技术
- 超分子化学 超分子化学
背景情况:
- 体自组装是创建纳米级功能材料的关键方法,通常通过β-sheet形成形成1D纤维状结构.
- 刺激反应性的自我组装是一个新兴的领域,灵感来自于自然的动态结构,用于创建可适应的材料.
研究的目的:
- 设计和描述一种新,可以自组装成具有葡萄糖结合能力的纳米线圈.
- 为了研究这些纳米线圈的葡萄糖诱导稳定和凝.
- 评估这些对葡萄糖反应的水凝在治疗药物,特别是治疗低血糖症的葡萄糖的潜在作用.
主要方法:
- 一个的合成功能化与酸 (PBA) 部分的葡萄糖结合.
- 使用显微镜技术对自组装纳米线圈形态的描述.
- 评估依赖葡萄糖的水凝形成和质性质.
- 在体外和体内评估葡萄糖封装和释放动力学在低血糖的小鼠模型.
主要成果:
- 设计的体自组装成一个不寻常的纳米线圈结构,通过葡萄糖结合稳定和延长.
- 葡萄糖结合诱导了纳米线圈纠和在生理学葡萄糖度下形成水凝.
- 从水凝中释放的葡萄糖与葡萄糖水平成反比例.
- 与对照组相比,与葡萄糖稳定的纳米线圈水凝显著改善了对小鼠严重急性低血糖的保护.
结论:
- 基于的纳米线圈与结合葡萄糖的酸基因可以形成刺激响应的水凝.
- 这些对葡萄糖反应敏捷的水凝为控制治疗剂的输送提供了一个有前途的平台,例如用于管理血糖水平的葡萄糖.
- 开发的系统在临床前的低血糖模型中显示出增强的治疗疗效.
相关概念视频
Protein Folding Quality Check in the RER
3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K
Oligosaccharide Assembly
2.9K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.9K
Protein Glycosylation
6.9K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
6.9K
Proteoglycans
3.9K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
3.9K


