Self-Assembled Protein Nanostructures via Irreversible Peptide Assembly.
ACS Macro Lett
; 12(12): 1679-1684, 2023 12 19.
Article
em En
| MEDLINE
| ID: mdl-38035369
ABSTRACT
The quaternary structure of proteins extends the functionality of monomeric proteins. Similarly, self-assembled protein nanostructures (SPrNs) have great potential to improve the functionality and complexity of proteins; however, the difficulty associated with the fabrication of SPrNs is far greater than that associated with the fabrication of self-assembled peptides or polymers and often requires sophisticated computational design. To make the process of SPrN formation simpler and more intuitive, herein, we devise a strategy to adopt an irreversible self-assembled peptide nanostructure (SPeN) process en route to the formation of SPrNs. The strategy employs three sequential steps:
first, the formation of SPeNs (an equilibrium process); second, covalent capture of SPeNs (an irreversible process); third, the final assembly of SPrNs via protein-peptide interactions (an equilibrium process). This strategy allowed us to fabricate SPrNs in which the size of the protein was approximately 9 times higher than that of the self-assembling peptide. Furthermore, we demonstrated that the irreversible SPeN could be used as a primary building block for assembly into superstructures. Overall, this strategy is conceptually as simple as SPeN fabrication and is potentially applicable to any soluble protein.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Nanoestruturas
Idioma:
En
Revista:
ACS Macro Lett
Ano de publicação:
2023
Tipo de documento:
Article