Abstract
‘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.
Keywords: Oral peptides, cyclization, aglycin, vglycin, cell-penetration, proteins.
Current Protein & Peptide Science
Title:The Disulfide Bond-Mediated Cyclization of Oral Peptides
Volume: 25 Issue: 6
Author(s): Chenguang Yao, Guoguo Ye, Qing Yang, Zhenwang Chen and Minghui Yang*
Affiliation:
- School of Life Science, Advanced Research Institute of Multidisciplinary Sciences; Key Laboratory of Molecular Medicine and Biotherapy, Key Laboratory of Medical Molecule Science and Pharmaceutics Engineering, Beijing Institute of Technology, Beijing, 100081, China
Keywords: Oral peptides, cyclization, aglycin, vglycin, cell-penetration, proteins.
Abstract: ‘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.
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Cite this article as:
Yao Chenguang, Ye Guoguo, Yang Qing, Chen Zhenwang and Yang Minghui*, The Disulfide Bond-Mediated Cyclization of Oral Peptides, Current Protein & Peptide Science 2024; 25 (6) . https://dx.doi.org/10.2174/0113892037280719231214095428
DOI https://dx.doi.org/10.2174/0113892037280719231214095428 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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