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Scientists uncover molecular architecture of self-organizing peptides on solid surfaces


The graphite-binding peptide and surface phenomena. The amino acid sequence of the dodecapeptide displays three chemically different domains and schematic representation of the possible surface phenomena. Molecular resolution AFM images of self-assembled peptide nanostructures, acquired in water. Credit: ACS Nano (2023). DOI: 10.1021/acsnano.2c10673
The graphite-binding peptide and surface phenomena. The amino acid sequence of the dodecapeptide displays three chemically different domains and schematic representation of the possible surface phenomena. Molecular resolution AFM images of self-assembled peptide nanostructures, acquired in water. Credit: ACS Nano (2023). DOI: 10.1021/acsnano.2c10673

A team of researchers from Kanazawa University in Japan and the University of Washington in Seattle have successfully uncovered the molecular architecture of a genetically designed peptide and its self-organization on atomically flat graphite surfaces. The study, which was published in the journal ACS Nano, utilized frequency modulated atomic force microscopy to reveal the molecular structure of the peptide, which forms single-molecule thick crystals on graphite surfaces.


Peptides are shorter chains of natural amino acids, compared to proteins, which can be hundreds and thousands of units long. Proteins are a vital building block for organisms, performing functions such as transporting ions, carrying out enzymatic reactions, and constituting the major structures of cells. The ability to predict a protein’s structure and function is crucial for designing drugs and vaccines, and understanding the origins of diseases.


Peptides, which have similar roles to proteins, have been considered less useful due to their disordered molecular structures and smaller sizes. However, by combining interdisciplinary approaches such as biology, engineering, and predictive modeling, researchers have turned the peptides’ “floppy” structures to their advantage.

Using a directed evolution approach, the team genetically engineered a graphite-binding peptide that has exclusive affinity to technological solids. The scientists demonstrated that the peptide predictably self-organizes on atomically flat graphite surfaces in patterns, which were predicted by computational modeling of the peptides.


Molecular recognition is the key to understanding how proteins carry out their functions. By recognizing their biological substrates, proteins can interact with DNA, proteins, enzymes, other biomolecules, or diseased cells. The scientists discovered that the graphite-binding peptide not only recognizes graphite atomic lattice but also forms its own molecular crystal, creating a coherent, continuous, soft interface between the peptide and the solid.


The scientists believe that their discovery will enable them to design hybrid biomolecular nanodevices for use in both biology and technology. Potential applications include bioelectronics, biosensors, protein arrays, and even logic devices. The teams are currently exploring further questions, such as the effects of mutations and structured water around peptides, and how they interact with other solid substrates. This research will establish the scientific foundations for the development of the next generation of biology-inspired technologies.


Journal Information:  Ayhan Yurtsever et al, Molecular Scale Structure and Kinetics of Layer-by-Layer Peptide Self-Organization at Atomically Flat Solid Surfaces, ACS Nano (2023). DOI: 10.1021/acsnano.2c10673
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