Fig. 7. Hierarchically oriented organization in peptide-containing co-assembly systems.

a | Long-range ordered nanofibre bundles assembled from a dipeptide (KK)–porphyrin co-assembly system due to the balance between electrostatic repulsion and van der Waals attraction¹¹³. b | Flat ribbons of 9-fluorenylmethyloxycarbonyl (Fmoc)–diphenylalanine (FF) and Fmoc–RGD co-assemblies comprising laterally aligned fine fibrils about 3 nm in diameter, as observed by fast Fourier transform analysis¹¹⁴. c | A protein–peptide co-assembly membrane containing elastin-like polypeptides and an amphiphilic peptide demonstrates pronounced nanofibrous multilayered architecture, as shown by scanning electron microscopy images of a cross-section of the membrane (top). The membrane can further evolve into tubular structures with simultaneously spatiotemporal control (bottom)¹¹⁶. d | Co-assembly of collagen-mimetic peptides (CP⁺⁺) and DNA origami yields the formation of nanowires with repeating periodicity of about 10 nm through face-to-face or edge-to-edge packing modes¹¹⁸. e | Bundles of intertwined fibres formed through co-assembly of DNA-mimetic peptide amphiphiles (top) and alkylated peptides (bottom)¹²⁵. Part a is adapted with permission from REF.¹¹³, Wiley-VCH. Part b is adapted with permission from REF.¹¹⁴, Elsevier. Part c is reproduced from REF.¹¹⁶, Springer Nature Limited. Part d is reproduced with permission from REF.¹¹⁸, ACS. Part e is reproduced with permission from REF.¹²⁵, AAAS.