聚-L-氨酸通过脂质双层的迁移
Fredric M Menger1, Victor A Seredyuk, Marina V Kitaeva
1Department of Chemistry, Emory University, Atlanta, Georgia 30322, USA. menger@emory.edu
Journal of the American Chemical Society
|March 6, 2003
概括
巨大的囊泡形成状结构与聚-l-lysines. 这些结构含有脂质和聚-l-lysines,解释药物输送到囊泡.
科学领域:
- 生物物理学的生物物理.
- 材料科学 材料科学 材料科学
- 纳米技术 纳米技术
背景情况:
- 巨型囊泡是细胞膜的模型系统.
- 聚-l-lysines是有潜在的生物医学应用的阴离子聚.
- 了解囊泡膜相互作用对于药物输送至关重要.
研究的目的:
- 研究与聚-l-lysines相互作用时巨型囊泡内的绳状结构的形成和组成.
- 为了阐明聚-l-氨酸进入囊泡的机制.
- 探索这些结构在调解药物透中的作用.
主要方法:
- 巨型囊泡制剂与中性和阴性脂质.
- 与不同分子量聚-l-lysines的相互作用研究.
- 光显微镜用光标记的脂质和聚-l-氨酸.
- 使用聚烯酸和光素异硫酸的微注射实验.
主要成果:
- 状结构在与聚-l-lysines接触时在囊泡内形成.
- 中性和离子脂质以及聚-l-lysine都是这些绳索的组成部分.
- 聚 (?? 烯酸) 诱导了绳索收缩,表明了聚/聚离子相互作用.
- 光标记的poly-l-lysine证实了它在绳索中的存在.
- 提出了一种涉及聚-l-氨酸结合,域形成和囊泡进入的模型.
结论:
- 聚-l-氨酸诱导了脂质囊泡中内部状结构的形成.
- 这些结构由脂质和聚-l-lysine组成,由静电相互作用介导.
- 拟议的模型解释了聚-l-氨酸在囊泡透和药物输送中的作用,例如多克索鲁比辛.
相关概念视频
02:43Peptide Bonds
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
01:26Membrane Fluidity
Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...
01:25Protein Glycosylation
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...
01:24Oligosaccharide Assembly
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...
01:10C–C Bond Formation: Aldol Condensation Overview
Aldol condensation is an important route in synthetic organic chemistry used to generate a new carbon–carbon bond under basic or acidic conditions. The aldol condensation reaction presented in Figure 1 constitutes an aldol addition reaction followed by the dehydration process.
01:19Formation of Lipopolysaccharides
Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...