Self-assembly of an amphipathic ααβ-tripeptide into cationic spherical particles for intracellular delivery

Abstract

The development of molecular carriers able to carry molecules directly into the cell is an area of intensive research. Cationic nanoparticles are effective delivery systems for several classes of molecules, such as anticancer agents, oligonucleotides and antibodies. Indeed, a cationic charge on the outer surface allows a rapid cellular uptake together with the possibility of carrying negatively charged molecules. In this work, we studied the self-assembly of an ultra-short ααβ-tripeptide containing an l-Arg-l-Ala sequence and an unnatural fluorine substituted β-diaryl-amino acid. The presence of the unnatural β-diaryl-amino acid allowed us to obtain a protease stable sequence. Furthermore, an arginine guanidinium group triggered the formation of spherical assemblies that were able to load small molecules and enter cells. These spherical architectures, thus, represent interesting candidates for the delivery of exogenous entities directly into cells.

Electrospinning of pyrazole-isothiazole derivatives: nanofibers from small molecules

“…The insertion of unnatural amino acids in the peptide sequences is a very established tool to overcome this problem. Starting from this consideration, and continuing our research on the preparation of non-coded amino acids and on their use to obtain peptidomimetics [24][25][26][27] for different applications ranging from biomedical application to nanomaterials, we investigated the electrospinnability of short peptide chains. In this work we used simple systems formed by natural amino acids coupled with an unnatural amino acid, i.e.…”

Self-assembled hydrophobic Ala-Aib peptide encapsulating curcumin: a convenient system for water insoluble drugs

“…11,23 Another signicant advantage in the use of non-coded amino acids is their capability to induce an increased stability in proteolytic environment. 24 Recently we reported on the preparation of short hydrophobic peptides able to create ordered supramolecular assemblies in water leading to the formation of nanocolloidal suspension. 25 The presence of the non-proteinogenic, cyclic, a,a 0 -substituted norbornene amino acid in a short peptide sequence (AcAla-NRB-Ala-Aib-AlaNH 2 1 and 2, Fig.…”

Surface Modification by Nano-Structures Reduces Viable Bacterial Biofilm in Aerobic and Anaerobic Environments

“…It arises through non-covalent interactions between components, including electrostatic, hydrophobic, hydrogen bonding and π-π interactions [ 29 ]. Depending on the specific building blocks and the assembly conditions, various nano-structured morphologies, including fibrils, tubes, sheets, tapes, spheres, vesicles and hydrogel matrices, can be formed in vitro, allowing for distinctive functional possibilities [ 28 , 30 , 31 , 32 , 33 , 34 , 35 ], mainly in tissue engineering [ 36 , 37 , 38 , 39 ], regenerative medicine [ 40 ], cell culture [ 41 , 42 , 43 , 44 ], drug delivery [ 36 , 39 , 45 , 46 , 47 , 48 , 49 ], bio-imaging [ 50 , 51 ] and fabric functionalization [ 52 ]. Coatings based on self-assembled peptides, primarily for antibacterial purposes, have been recently reported [ 5 , 12 , 13 , 21 , 53 , 54 , 55 , 56 ].…”