The aliphatic dipeptide alanine–isoleucine (Ala–Ile), protected with a benzyl­oxycarbonyl (Z) group at the N-terminus, forms hollow microtubes with ortho­rhom­bic symmetry upon evaporation on glass surfaces, as shown by field emission scanning electron microscopy (FESEM). These findings provide an increased understanding of the correlation between the single-crystal structure of the peptide building block and its self-assembly mechanism, and expand the library of available building blocks for microtechnological applications.