Self-assembled Structures from Amphiphilic Peptides

Abstract

Nanotechnology and its applications are strongly influenced by structures self-assembled from a variety of different materials. This review covers nanostructures, including micelles, rod-like micelles, fibers and peptide beads, self-assembled from de novo designed amphiphilic peptides. The latter are promising candidates for the development of nanoscale carrier systems because they are completely composed of amino acids. In addition to designing primary sequences, secondary structure and external parameters are also discussed with respect to their impact on self-assembly. Moreover, the assembly process itself is examined. Potential applications range from gene and drug delivery devices to diagnostics, thereby highlighting the versatility of the system.

Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptide

“…It is noteworthy that β‐sheet to hydrogel transitions have previously been observed . Accordingly, we visually observed, at concentrations >10 mM in water or in a mixture of water/acetonitrile (or DMSO), the formation of a rigid hydrogel.…”

Delivery of ROS Generating Anthraquinones Using Reduction‐Responsive Peptide‐Based Nanoparticles

“…As the peptide NPs are MCMs, they possess multiple hydrophobic inner cores and thus preferentially entrap hydrophobic compounds. [ ][ ] Therefore, the structural differences between these anthraquinones can affect their loading efficiency within the hydrophobic cores of the peptide NPs. To prepare the loaded NPs, the anthraquinone was added to a peptide solution, diluted to a final concentration of 6 – 12 μ m in 50% ethanol and dialyzed against water.…”

“…More complex self‐assembly structures, namely multi‐compartment‐micelles (MCMs) can host both hydrophilic and hydrophobic drugs, making them especially versatile candidates for drug delivery. We have recently reported the redox‐responsive amphiphilic peptide H 3 SSgT (of the sequence H 2 N ‐H 3 ‐X‐[W‐ D L] 3 ‐W‐ NH 2 , where X = –NH‐(CH 2 ) 2 ‐S‐S‐(CH 2 ) 2 ‐NH‐CO‐(CH 2 ) 2 ‐CO– and D L = d ‐Leucine; Figure ), that forms such MCMs . They were shown to efficiently entrap the model compound boron‐dipyrromethene (Bodipy) and release it in presence of physiological amounts of reducing agent .…”

Prediction of Amphiphilic Cell-Penetrating Peptide Building Blocks from Protein-Derived Amino Acid Sequences for Engineering of Drug Delivery Nanoassemblies

“…9 The structures produced with synthetic peptides, such as K3-(WL)3-W-NH 2 ), C 16 -WAAAAKAAAAKAAAAK), or C 18 -KTTKS, have been in agreement with the molecular shape concept of the critical packing parameter, which determines the type of the obtained aggregates (micelles, vesicles or nanotube rods). [66][67][68]71,72,83,84 Some studies have yielded ambiguous conclusions about the topology of the self-assembled peptide scaffolds because the Israelachvili's prediction does not account for the intermolecular interactions between α-helical moieties nor for the hydrogen bonding interactions between peptides of β-sheet conformations. 4,13,34,75,80 The initially proposed numerical approaches for CPP prediction have mainly been based on trial and error methods.…”