What is it about?
we reported the formation of peptide 3D crystals on solids through a layer-by-layer (LBL) peptide self-assembly, mimicking the constructions of natural layered minerals such as graphite, MoS2 and mica. Peptides at each layer enable the formation of well-organized supramolecular arrays or 2D crystal patterns. The interlayer distance of peptide 3D crystal maintained the same, affecting by specific peptide sequences and substrates. Moreover, the orientations of the upper peptide layer followed the same direction of the lower peptide layer. Unlike solid lattice with the exact same atomic arrangement, the peptide 1st layer confined by the underlying substrate showed different repeating unit cells in comparison to the upper peptide layers found by high-resolution in situ AFM measurements. Besides, we investigated the effect of concentration, substrate and solvent on the formation of peptide 3D crystals.
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Why is it important?
Coupling biomolecules and two-dimensional (2D) nanomaterials have found great applications for bioelectronics, biosensing and bioengineering. Peptide self-assembly on 2D nanomaterials is currently being widely studied via forming monolayer molecular scaffolds on solids.
Perspectives
Such LBL peptide construction also provides a good advantage for electron transportation between the peptide 1st layer-nanomaterials and interpeptide layers. This work would shed lights on next-generation bionanodevices and protein crystal engineering.
Linhao Sun
Kanazawa Daigaku
Read the Original
This page is a summary of: Formation of stacked 3D crystals of self-assembled peptides via mimicking construction of layered natural minerals, Journal of Colloid and Interface Science, February 2026, Elsevier,
DOI: 10.1016/j.jcis.2025.139146.
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