Supramolecular Interactions and Morphology of Self-Assembling Peptide Amphiphile Nanostructures.
The morphology of supramolecular peptide nanostructures is difficult to predict given their complex energy landscapes. We investigated peptide amphiphiles containing β-sheet forming domains that form twisted nanoribbons in water. We explained the morphology based on a balance between the energetically favorable packing of molecules in the center of the nanostructures, the unfavorable packing at the edges, and the deformations due to packing of twisted β-sheets. We find that morphological polydispersity of PA nanostructures is determined by peptide sequences, and the twisting of their internal β-sheets. We also observed a change in the supramolecular chirality of the nanostructures as the peptide sequence was modified, although only amino acids with l-configuration were used. Upon increasing charge repulsion between molecules, we observed a change in morphology to long cylinders and then rodlike fragments and spherical micelles. Understanding the self-assembly mechanisms of peptide amphiphiles into nanostructures should be useful to optimize their well-known functions.
['Sangji|M Hussain|MH|0000-0002-4205-2541', 'Sai|Hiroaki|H|0000-0002-4268-2148', 'Chin|Stacey M|SM|0000-0002-2909-6080', 'Lee|Sieun Ruth|SR|', 'R Sasselli|Ivan|I|0000-0001-6062-2440', 'Palmer|Liam C|LC|0000-0003-0804-1168', 'Stupp|Samuel I|SI|0000-0002-5491-7442']
D000595:Amino Acid Sequence D000596:Amino Acids D049329:Nanostructures D010455:Peptides D014867:Water
self-assembly peptide amphiphile nanostructure supramolecular chirality