Modification of Low-Energy Surfaces Using Bicyclic Peptides Discovered by Phage Display.
J Am Chem Soc
; 145(32): 17613-17620, 2023 08 16.
Article
en En
| MEDLINE
| ID: mdl-37531461
ABSTRACT
Solid-binding peptides are a simple and versatile tool for the non-covalent modification of solid material surfaces, and a variety of peptides have been developed by reference to natural proteins or de novo design. Here, for the first time, we report the discovery of a bicyclic peptide targeting the heterogeneous material polypropylene by combining phage display technology and next-generation sequencing. We find that the enrichment properties of bicyclic peptides capable of binding to polypropylene are distinct from linear peptides, as reflected in amino acid abundance and a trend toward negative net charges and high hydrophobicity. The selected bicyclic peptide has a higher binding affinity for polypropylene compared with a previously reported linear peptide, enabling the hydrophilic and adhesive properties of the polypropylene to be more effectively enhanced. Our work paves the way for the exploration and utilization of conformational-restricted cyclic peptides as a new family of functionally evolvable agents for material surface modification.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Polipropilenos
/
Bacteriófagos
Idioma:
En
Revista:
J Am Chem Soc
Año:
2023
Tipo del documento:
Article
País de afiliación:
China