当前位置: X-MOL 学术Curr. Protein Pept. Sci. › 论文详情
Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)
The Disulfide Bond-Mediated Cyclization of Oral Peptides
Current Protein & Peptide Science ( IF 2.8 ) Pub Date : 2024-01-25 , DOI: 10.2174/0113892037280719231214095428
Chenguang Yao 1 , Guoguo Ye 2, 3 , Qing Yang 4 , Zhenwang Chen 5 , Minghui Yang 6
Affiliation  

‘Structure determines function’ is a consensus in the current biological community, but the structural characteristics corresponding to a certain function have always been a hot field of scientific exploration. A peptide is a bio-active molecule that is between the size of an antibody and a small molecule. Still, the gastrointestinal barrier and the physicochemical properties of peptides have always limited the oral administration of peptides. Therefore, we analyze the main ways oral peptide conversion strategies of peptide modification and permeation enhancers. Based on our analysis of the structure of natural oral peptides, which can be absorbed through the gastrointestinal tract, we believe that the design strategy of natural stapled peptides based on disulfide bonds is good for oral peptide design. This cannot only be used to identify anti-gastrointestinal digestive structural proteins in nature but also provide a solid structural foundation for the construction of new oral peptide drugs.

中文翻译:

二硫键介导的口服肽环化

“结构决定功能”是当前生物界的共识,但某种功能对应的结构特征一直是科学探索的热点领域。肽是一种生物活性分子,其大小介于抗体和小分子之间。尽管如此,胃肠道屏障和肽的理化性质一直限制着肽的口服给药。因此,我们分析了口服肽转化策略的主要方式为肽修饰和渗透促进剂。基于我们对可通过胃肠道吸收的天然口服肽的结构的分析,我们认为基于二硫键的天然钉合肽的设计策略有利于口服肽的设计。这不仅可以用于鉴定自然界中的抗胃肠道消化结构蛋白,还可以为新型口服肽药物的构建提供坚实的结构基础。
更新日期:2024-01-25
down
wechat
bug