What is it about?
We utilized the synthetic fibroin-like peptides with sequences of NH2–Y(GA)n=3–5Y–COOH to investigate the morphological and structural characteristics, molecular orientations, and single molecule structures on MoS2 under different time and concentration conditions. This work would expand potential applications using fibroin-like peptide-based nanodevices for biosensing and bioelectronics.
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Why is it important?
The formation of strong intermolecular hydrogen-bonding networks among repeating key motifs, i.e., Glu-Ala motifs of silk fibroin proteins, providing excellent mechanical and biochemical properties, has gained broad attention in many fields. For example, in biosensing, they could be utilized as stable molecular scaffolds on layered nanomaterials such as MoS2 for high-sensitivity targeting-molecule detection. However, understanding the characteristics of self-assembled fibroin-like proteins, i.e., concentration-/time-dependent morphological and structural changes, on the solids is still poor.
Perspectives
We would like to utilize the self-assembled Y(GA)nY peptides to functionalize single layer MoS2 or graphene for various nanodevices such as biosensing and bioelectronics. The monolayer-thick silk peptide patterns with high stiffness have the potential to be used as a matrix for studying cell activities such as cell division or cell development. Besides, it can be used as a medium for application in the brain–machine interface.
Linhao Sun
Kanazawa Daigaku
Read the Original
This page is a summary of: Structural Ordering of Interfacially Assembled Silk Fibroin-Like Peptides via Robust Intermolecular Hydrogen-Bonding Networks, ACS Materials Letters, July 2024, American Chemical Society (ACS),
DOI: 10.1021/acsmaterialslett.4c01045.
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