New RGD-peptide amphiphile mixtures containing a negatively charged diluent

Abstract

Here, we studied the self-assembly of two peptide amphiphiles, C16-Gly-Gly-Gly-Arg-Gly-Asp (PA 1: C16-GGG-RGD) and C16-Gly-Gly-Gly-Arg-Gly-Asp-Ser (PA 2: C16-GGG-RGDS). We showed that PA 1 and PA 2 self-assemble into nanotapes with an internal bilayer structure. C16 chains were highly interdigitated within the nanotape cores, while the peptide blocks formed water-exposed 13-sheets too. PA 1 nanotapes were characterized by one spacing distribution, corresponding to a more regular internal structure than that of PA 2 nanotapes, which presented two different spacing distributions. We showed that it is possible to obtain homogeneous nanotapes in water by co-assembling PA 1 or PA 2 with the negatively charged diluent C,16-Glu-Thr-Thr-Glu-Ser (PA 3: C16-ETTES). The homogeneous tapes formed by PA 1-PA 3 or PA 2-PA 3 mixtures presented a structure similar to that observed for the corresponding pure PA 1 or PA 2 nanotapes. The mixed nanotapes, which were able to form a stabilized matrix containing homogeneously distributed cell adhesive RGD groups, represent promising materials for designing new cell adhesion substrates.

Self-Assembly and Anti-Amyloid Cytotoxicity Activity of Amyloid beta Peptide Derivatives

“…The first uses ANS, the fluorescence of which depends on the hydrophobic environment3233343536. The second uses ThT, which is sensitive to the formation of amyloid fibrils3237383940.…”

Self-assembly of biomolecular soft matter

“…Papers from the groups of Jan van Hest/Lowik, 107 Mazza/Kostarelos, 108 Saiani, 109 Adams, 110 and Hamley 111 demonstrated the richness of these molecules given their programmable secondary structure and also their potential biomedical translation. Strong evidence was presented from solid state NMR, x-ray diffraction, and circular dichroism for the internal arrangement of peptide amphiphiles in flat nanostructures.…”

“…107 It was also clear from these papers how complex is the assembly of peptides into gels even when molecules are as simple as dipeptides and octapeptides, 109, 110 and intriguing how a single amino acid in a terminal bioactive epitope of a peptide amphiphile can change the supramolecular energy landscape yielding different periodicities in the assembly. 111 On the functional side, the paper by Mazza/Kostarelos showed at the Discussion that cationic peptide amphiphile nanofibers can be internalized by neurons and can also degrade in the brain. 108 One intriguing point linked to this paper is the question of whether or not the supramolecular nanofibers could cross the blood brain barrier.…”

Self‐assembling amphiphilic peptides

“…Pyrene is a fluorescent probe molecule that is used to locate the CAC for conventional amphiphiles, as its fluorescence is sensitive to the local hydrophobic environment [27,28]. It has also successfully been used to determine the CAC for several PA systems [12,21,[29][30][31][32][33][34][35]. In contrast to this method, the fluorescence of thioflavin T is dependent on the formation of amyloid-like structures (β-sheet fibrils) [36,37] and has been used for amyloid fibril-forming peptides.…”