来自Polygonatum kingianum的多糖的化学结构和免疫调节活动
Nanyu Chen1, Yunzhang Ding2, Xuan Li3
1Institute for Inheritance-Based Innovation of Chinese Medicine, School of Pharmacy, Shenzhen University Medical School, Shenzhen University, Shenzhen 518060, China; State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China.
International journal of biological macromolecules
|September 8, 2024
概括
从Polygonatum kingianum根茎中分离出来的三种果实具有良好的热稳定性和独特的结构. 其中两个多糖 (PKP-1和PKP-2) 通过激活NF-κB信号通路,显示出潜在的免疫调节活性.
科学领域:
- 食品科学 食品科学 食品科学
- 药用化学 医学化学
- 生物化学 生化学
背景情况:
- 中国药草Polygonatum kingianum被用于食品和医药,但其多糖的特性尚未得到充分研究.
- 多糖是复杂的碳水化合物,具有多样化的生物活动和在食品和制药中的应用.
研究的目的:
- 从Polygonatum kingianum根茎中分离和描述多糖类.
- 研究它们的物理化学性质,包括结构,热稳定性和风湿学.
- 为了在体外评估它们的潜在免疫调节活性.
主要方法:
- 聚糖的分离和净化 (PKP-1, PKP-2, PKP-3).
- 使用糖酸键类型的确定进行结构分析.
- 物理化学表征:分子量,SEM,热分析,风学.
- 在实验室对巨细胞的免疫调节试验 (NO,TNF-α,通过NF-κB通路分泌IL-6).
主要成果:
- 分离了三种具有不同分子重量的果糖素 (PKP-1,PKP-2,PKP-3).
- 结构分析显示了特定的β-D-Fruf和α-D-Glcp糖化链接;PKP-2含有乙基和曼诺斯残留物.
- 多糖体表现出良好的热稳定性,独特的形态和剪切稀释流体行为.
- 通过激活NF-κB通路,PKP-1和PKP-2显著增强了巨细胞中的NO和细胞因子分泌.
结论:
- 波利格纳 (Polygonatum kingianum) 的多糖主要是果糖,具有不同的物理化学性质.
- PKP-1和PKP-2具有显著的免疫调节潜力,这表明其在功能性食品中的应用.
- 这项研究为在食品工业中利用Polygonatum多糖提供了基础.
相关概念视频
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
Glycosaminoglycans
4.8K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
4.8K
Cellulose and Pectic Polysaccharides
3.5K
Every plant cell has a cell wall that protects the cell, provides structural support, and gives the cell shape. Cellulose, the main structural component of the plant cell wall, makes up over 30% of plant matter. It is the most abundant organic compound on earth. Cellulose is an unbranched polysaccharide composed of linear chains of glucose molecules linked by β (1→4) glycosidic bonds.
As a cell matures, its cell wall specializes according to its type. For example, the...
As a cell matures, its cell wall specializes according to its type. For example, the...
3.5K
Glycocalyx and its Functions
3.7K
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
3.7K
Protein Glycosylation
6.8K
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...
6.8K
Oligosaccharide Assembly
2.8K
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...
2.8K


