Cargando…
Artificial disulfide-rich peptide scaffolds with precisely defined disulfide patterns and a minimized number of isomers
Disulfide-rich peptides are emerging as potential templates for drug design applications. However, the synthesis and reengineering of disulfide-rich peptides are challenging, owing to the complexity of the oxidative folding process involving a number of diverse isomeric structures. Novel disulfide-r...
Autores principales: | Zheng, Yiwu, Li, Zhuoru, Ren, Jing, Liu, Weidong, Wu, Yaqi, Zhao, Yibing, Wu, Chuanliu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431680/ https://www.ncbi.nlm.nih.gov/pubmed/28553486 http://dx.doi.org/10.1039/c6sc05710a |
Ejemplares similares
-
De novo design of constrained and sequence-independent peptide scaffolds with topologically-formidable disulfide connectivities
por: Zheng, Yiwu, et al.
Publicado: (2017) -
An evolution-inspired strategy to design disulfide-rich peptides tolerant to extensive sequence manipulation
por: Zha, Jun, et al.
Publicado: (2021) -
Selection and evolution of disulfide-rich peptides via cellular protein quality control
por: Meng, Xiaoting, et al.
Publicado: (2023) -
De novo design and directed folding of disulfide-bridged peptide heterodimers
por: Yao, Sicong, et al.
Publicado: (2022) -
Structure-guided design of CPPC-paired disulfide-rich peptide libraries for ligand and drug discovery
por: Wu, Yapei, et al.
Publicado: (2022)