Self-assembled light-harvesting peptide nanotubes for mimicking natural photosynthesis

Light-harvesting peptide nanotubes are synthesized by the self-assembly of diphenylalanine with THPP and platinum nanoparticles (nPt; see picture; TEOA = triethanolamine). The light-harvesting peptide nanotubes are suitable for mimicking photosynthesis because of their structure and electrochemical properties that are similar to the ones of photosystem?I in natural photosynthesis.     

Interactions of KLVFF-PEG peptide conjugate with fibrinogen in neutral aqueous solutions

In this work we report on the interaction of KLVFF-PEG with fibrinogen (Fbg) in neutral aqueous solutions at 20 degrees C, for particular ratios of KLVFF-PEG to Fbg concentration, Delta = c(KLVFF-PEG)/c(Fbg). Our results show the formation of Fbg/KLVFF-PEG complexes for Delta > 0, such that there is not an extended network of complexes throughout the solution. In addition, cleaved protein and Fbg dimers are identified in the solution for Delta >or= 0. There is a dramatic change in the tertiary structure of the Fbg upon KLVFF-PEG binding, although the KLVFF-PEG binds to the Fbg without affecting the secondary structure elements of the glycoprotein.     

Tetrapeptidic Molecular Hydrogels: Self‐assembly and Co‐aggregation with Amyloid Fragment Aβ1‐40

A new family of isomeric tetrapeptides containing aromatic and polar amino acid residues that are able to form molecular hydrogels following a smooth change in pH is described. The hydrogels have been studied by spectroscopic and microscopic techniques showing that the peptide primary sequence has an enormous influence on the self‐assembly process. In particular, the formation of extended hydrophobic regions and the appearance of π‐stacking interactions have been revealed as the driving forces for aggregation. Moreover, the interaction of these compounds with amyloid peptidic fragment Aβ1‐40 has been studied and some of them have been shown to act as templates for the aggregation of this peptide into non‐β‐sheet fibrillar structures. These compounds could potentially be used for the capture of toxic, soluble amyloid oligomers.     

Honeycomb self-assembled peptide scaffolds by the breath figure method

The self-assembly of molecules into desired architectures is currently a challenging subject for the development of supramolecular chemistry. Here we present a facile "breath figure" assembly process through the use of the self-assembled peptide building block diphenylalanine (L-Phe-L-Phe, FF). Macroporous honeycomb scaffolds were fabricated, and average pore size could be regulated, from (1.00±0.18) μm to (2.12±0.47) μm, through the use of different air speeds. It is indicated that the honeycomb formation is humidity-, solvent-, concentration-, and substrate-dependent. Moreover, water molecules introduced from "breath figure" intervene in the formation of hydrogen bonds during FF molecular self-assembly, which results in a hydrogen bond configuration transition from antiparallel β sheet to parallel β sheet. Meanwhile, as a result of the higher polarity of water molecules, the FF molecular array is transformed from laminar stacking into a hexagonal structure. These findings not only elucidate the FF molecule self-assembly process, but also strongly support the mechanism of breath figure array formation. Finally, human embryo skin fibroblast (ESF) culture experiments suggest that FF honeycomb scaffolds are an attractive biomaterial for growth of adherent cells with great potential applications in tissue engineering.     

Reversible transitions between peptide nanotubes and vesicle-like structures including theoretical modeling studies

Peptide-based self-assembling systems are increasingly attractive because of their wide range of applications in different fields. Peptide nanostructures are flexible with changes in the ambient conditions. Herein, a reversible shape transition between self-assembled dipeptide nanotubes (DPNTs) and vesicle-like structures is observed upon a change in the peptide concentration. SEM, TEM, AFM, and CD spectroscopy were used to follow this transition process. We show that dilution of a peptide-nanotube dispersion solution results in the formation of vesicle-like structures, which can then be reassembled into the nanotubes by concentrating the solution. A theoretical model describing this shape-transition phenomenon is presented to propose ways to engineer assembling molecules in order to devise other systems in which the morphology can be tuned on demand.