Programming two-component peptide self-assembly by tuning the hydrophobic linker.

Molecular self-assembly enables the formation of intricate networks through non-covalent interactions, serving as a key strategy for constructing structures ranging from molecules to macroscopic forms. While zero-dimensional and one-dimensional nanostructures have been widely achieved, two-dimensional nanostrip structures present unique advantages in biomedical and other applications due to their high surface area and potential for functionalization. However, their efficient design and precise regulation remain challenging. This study systematically explores how different hydrophobic amino acid linkers impact the microscopic morphology in two-component co-assembly systems with strong electrostatic interactions. The introduction of the AA linker resulted in distinctive 2D nanostrips, which stacked to form bilayer sheets, whereas VV, LL, and NleNle linkers formed one-dimensional fibers. In contrast, GG and PP linkers did not produce stable aggregates. Our findings highlight the role of intermolecular interactions in the development of 2D assemblies, providing new insights into the design and application of 2D materials.