Biomimetic folding strategies for chemical synthesis of disulfide-bonded peptides and proteins.
Chembiochem
; : e202400674, 2024 Oct 02.
Article
in En
| MEDLINE
| ID: mdl-39356249
ABSTRACT
Disulfide-bonded peptides and proteins, including hormones, toxins, growth factors, and others, are abundant in living organisms. These molecules play crucial physiological roles such as regulating cell and organism growth, development, and metabolism. They have also found widespread applications as drugs or tool molecules in biomedical and pharmaceutical research. However, the chemical synthesis of disulfide-bonded proteins is complicated by the challenges associated with their folding. This review focuses on the latest advancements in disulfide-bonded peptide and protein folding technologies. Particularly, it highlights biomimetic folding strategies that emulate the naturally occurring oxidative folding processes in nature. These strategies include chaperone-assisted folding, glycosylation-assisted folding, and organic-based oxidative folding methods. The review also anticipates future directions in folding technology. Such research offers innovative approaches for the chemical synthesis of complex proteins that are otherwise difficult-to-fold.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Language:
En
Journal:
Chembiochem
Journal subject:
BIOQUIMICA
Year:
2024
Document type:
Article
Affiliation country:
China
Country of publication:
Germany