Heterogeneous and Cooperative Rupture of Histidine-Ni2+ Metal-Coordination Bonds on Rationally Designed Protein Templates.
ACS Biomater Sci Eng
; 10(5): 2945-2955, 2024 05 13.
Article
en En
| MEDLINE
| ID: mdl-38669114
ABSTRACT
Metal-coordination bonds, a highly tunable class of dynamic noncovalent interactions, are pivotal to the function of a variety of protein-based natural materials and have emerged as binding motifs to produce strong, tough, and self-healing bioinspired materials. While natural proteins use clusters of metal-coordination bonds, synthetic materials frequently employ individual bonds, resulting in mechanically weak materials. To overcome this current limitation, we rationally designed a series of elastin-like polypeptide templates with the capability of forming an increasing number of intermolecular histidine-Ni2+ metal-coordination bonds. Using single-molecule force spectroscopy and steered molecular dynamics simulations, we show that templates with three histidine residues exhibit heterogeneous rupture pathways, including the simultaneous rupture of at least two bonds with more-than-additive rupture forces. The methodology and insights developed improve our understanding of the molecular interactions that stabilize metal-coordinated proteins and provide a general route for the design of new strong, metal-coordinated materials with a broad spectrum of dissipative time scales.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Simulación de Dinámica Molecular
/
Histidina
/
Níquel
Idioma:
En
Revista:
ACS Biomater Sci Eng
Año:
2024
Tipo del documento:
Article
País de afiliación:
Estados Unidos