14 research outputs found
Peptide–Graphene Interactions Enhance the Mechanical Properties of Silk Fibroin
Studies reveal that biomolecules
can form intriguing molecular structures with fascinating functionalities
upon interaction with graphene. Then, interesting questions arise.
How does silk fibroin interact with graphene? Does such interaction
lead to an enhancement in its mechanical properties? In this study,
using large-scale molecular dynamics simulations, we first examine
the interaction of graphene with several typical peptide structures
of silk fibroin extracted from different domains of silk fibroin,
including pure amorphous (P1), pure crystalline (P2), a segment from
N-terminal (P3), and a combined amorphous and crystalline segment
(P4), aiming to reveal their structural modifications. Our study shows
that graphene can have intriguing influences on the structures formed
by the peptides with sequences representing different domains of silk
fibroin. In general, for protein domains with stable structure and
strong intramolecular interaction (e.g., β-sheets), graphene
tends to compete with the intramolecular interactions and thus weaken
the interchain interaction and reduce the contents of β-sheets.
For the silk domains with random or less ordered secondary structures
and weak intramolecular interactions, graphene tends to enhance the
stability of peptide structures; in particular, it increases the contents
of helical structures. Thereafter, tensile simulations were further
performed on the representative peptides to investigate how such structure
modifications affect their mechanical properties. It was found that
the strength and resilience of the peptides are enhanced through their
interaction with graphene. The present work reveals interesting insights
into the interactions between silk peptides and graphene, and contributes
in the efforts to enhance the mechanical properties of silk fibroin