Solvent and surface controlled self-assembly of diphenylalanine peptide: from microtubes to nanofibers

Peptide Self-Assembled Nanostructures for Drug Delivery Applications

“…Amphiphilic peptides have many different types such as linear peptides, ionic complementary peptides, peptide phospholipids, and long-chain alkylated peptides [68,69]. Amphiphilic peptides are generally formed from hydrophilic peptide head groups and hydrophobic tails that could be used to form various secondary and tertiary conformations [70,71].…”

“…Amphiphilic peptides are generally formed from hydrophilic peptide head groups and hydrophobic tails that could be used to form various secondary and tertiary conformations [70,71]. These peptides could selfassemble into nanostructures with many different morphological structures including nanovesicles, nanotubules, and nanomicelles [69,72]. The electrostatic and hydrophobic interactions are thought to be the main factors that drive the self-assembly for amphiphilic peptides [73].…”

Self-assembled peptide nanomaterials for biomedical applications: promises and pitfalls

“…10 Inspired by lipid molecules in cell membranes, pure peptides with hydrophobic tails and hydrophilic heads can self-assemble into nanotubes, nanovesicles, and micelles, depending both on their chemical properties (eg, peptide sequences, charges, concentration, etc) and physical properties (eg, size, shape, etc). [15][16][17] For the hydrophobic tail (which normally contains six residues), amino acids such as G, A, V, L, I, and F are good candidates; meanwhile, D, K, E, R, and H are used in the hydrophilic domain. 10,18,19 For example, similar 24 discovered the first self-assembling peptide EAK16 (n-AEAEAKAKAEAEAKAK-c) that formed into nanofibers.…”

“…The sequence with PEO promoted the highest fibroblast cell adhesion and growth, which could be used to develop a membrane system to screen biological probes for cell adhesion and growth. Later on, Lin et al synthesized pH-sensitive ampiphilic peptides C 16 GSH and C 16 EOSH composed of histidine and serine with a single fatty acid tail and branched structure. 77 Using histidine as the switch, these peptides were viscoelastic liquids at a pH value ,5.5.…”

Self-assembly of surfactant-like peptides and their applications

“…As examples, ultrashort SLPs containing three or four residues such as Ac-IVD and Ac-IIIK-NH 2 have been found to readily selfassemble into long fibers in water [46,47]; A 6 K shows high solubility in water up to ~12 wt% and forms a nematic phase consisting of long assembled nanotubes at ~17 wt% [48]. Although some short FF-containing peptides (e.g., FF and KLVFFAE) can also form long tubes or fibers, they show poor water solubility and their self-assembly in aqueous solutions is usually realized by adding organic solvents such as 1,1,1,3,3,3-hexafluoro-2-propanol or acetonitrile [9,[35][36][37]70]. As shown in Table 1, the range of self-assembling peptide building blocks is so wide that it would be impossible to cover the entire spectrum in a single article.…”