Co-assembled Coiled-Coil Peptide Nanotubes with Enhanced Stability and Metal-Dependent Cargo Loading

Abstract

Peptide nanotube biomaterials are attractive for their range of applications. Herein, we disclose the co-assembly of coiled-coil peptides, one with ligands for metal ions that demonstrate hierarchical assembly into nanotubes, with spatial control of the metal-binding ligands. Enhanced stability of the nanotubes to phosphate-buffered saline was successfully accomplished in a metal-dependent fashion, depending on the levels and placement of the ligand-containing coiled-coil peptide. This spatial control also allowed for site-specific labeling of the nanotubes with His-tagged fluorophores through the length of the tubes or at the termini, in a metal-dependent manner.

Recent advances in coiled-coil peptide materials and their biomedical applications

“…74 A second generation of these nanotubes was created to stabilize the tubes and thereby expand the scope of this material as a delivery vehicle. 75 By introducing metal-binding ligands into this nanotube using heterotrimers composed of the coiled-coil peptides p2L ( vide supra ) and TriNL , the tube stability was increased in a metal-dependent manner. These tubes were still able to include dextrans within their interior, with inclusion of His-tagged fluorophores at either the ends of the tubes, or throughout, with the addition of metal ions.…”

Peptide-Based Low Molecular Weight Photosensitive Supramolecular Gelators

“…These newly generated multicomponent co-assembled systems give access to tailored features, enhanced mechanical and architectural scope, desired morphology, improved bioavailability, and functional complexity with emergent behavior [ 48 , 49 , 50 , 51 , 52 , 53 , 54 , 55 , 56 , 57 , 58 , 59 ]. In fact, in recent years, a considerable amount of effort have been dedicated in the direction of designing peptide-based multicomponent systems decorated with desired structures, properties, and functions with multitasking abilityies via co-assembly, which is difficult for a monocomponent peptide assembly to realize [ 48 , 57 , 58 , 59 , 60 , 61 ].…”