自组装具有类似胰岛素的生长因子仿真
Abhishek Roy1, Joseph B Dodd-O1, Alicia S Robang2
1Department of Biomedical Engineering, New Jersey Institute of Technology, Newark, New Jersey 07102, United States.
ACS applied materials & interfaces
|December 25, 2023
概括
这项研究引入了自我组装的基,模仿胰岛素类生长因子 (IGF) 信号传输. 这些新型生物材料为组织工程和药物设计中的潜在治疗应用提供了更好的准和稳定性.
科学领域:
- 生物材料科学 生物材料科学
- 再生医学是一种再生医学.
- 分子信号传输的方法
背景情况:
- 增长因子 (GF) 仿真旨在复制自然信号分子的功能.
- 目前的GF模仿在目标传递和受体结合稳定性方面面临挑战.
- 自组装 (SAP) 提供了一个潜在的平台来克服这些局限性.
研究的目的:
- 开发合成的,自组装的生长因子 (GFs),模仿胰岛素类生长因子 (IGF) 信号传递.
- 为增强的GF模拟应用创造生物相容的水凝.
- 为了应对针对性交付和长期稳定性GF模拟的挑战.
主要方法:
- 使用自组合 (SAP) 平台创建合成IGF信号GFs.
- 具有已证明生物相容性的制造型基.
- 评估了水凝与IGF受体的结合,亲血管性信号激活和体外血管生成.
主要成果:
- 类水凝表现出剂量依赖的结合,以准IGF受体.
- 激活了亲血管性信号通路,并在体外促进了血管性微管的形成.
- 透水凝的长期稳定性已被证明,持续数周到数月.
结论:
- 开发出稳定,自我组装的基,模仿IGF信号传递.
- SAP/GF仿真植入物的增强准和延长稳定性.
- 在未来的GF模仿疗法中,有可能提高疗效和安全性.
相关概念视频
Insulin: Biosynthesis, Chemistry, and Preparation
385
The endoplasmic reticulum (ER) of pancreatic β-cells synthesizes preproinsulin, which consists of a signal peptide, A and B chains, and a C-peptide. Preproinsulin is then cleaved and folded into proinsulin, which translocates to the Golgi apparatus for sorting and packaging into secretory granules. In these granules, enzymatic clipping generates insulin and C-peptide.
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment...
Damage or functional impairment of β-cells inhibits insulin production, leading to diabetes. Diabetes treatment...
385
Glucagon-like Receptor Agonists
327
Incretins include glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which stimulate insulin secretion post-meals. In type 2 diabetes, GIP's efficacy is reduced, making GLP-1 a viable drug target. GIP originates from preproGIP.
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by...
GLP-1, when administered in high doses intravenously, triggers insulin secretion, inhibits glucagon release, slows gastric emptying, reduces food intake, and restores normal insulin secretion. However, its rapid inactivation by...
327
Protein and Protein Structure
79.6K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.6K
Insulin Secretory Vesicles
5.0K
Insulin secretory vesicles release insulin to stimulate blood glucose uptake and regulate carbohydrate metabolism. When the blood glucose levels increase, glucose enters the pancreatic β-islet cells through glucose transporters. Once inside, glucose is metabolized through glycolysis, the citric acid cycle, and the electron transport chain, producing ATP. This increase in ATP concentration closes ATP-sensitive potassium channels, leading to depolarization of the membrane and the opening of...
5.0K
Insulin: The Receptor and Signaling Pathways
1.2K
Insulin action is mediated through a receptor tyrosine kinase, akin to the IGF-1 receptor. The number of receptors per cell varies significantly, from 40 on erythrocytes to 300,000 on adipocytes and hepatocytes. The insulin receptor consists of linked α/β subunit dimers, forming a heterotetramer glycoprotein with two extracellular α subunits and two β subunits spanning the membrane. The α subunits inhibit the inherent tyrosine kinase activity of the β subunits, but...
1.2K
Protein Complex Assembly
10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K


