Control of peptide nanotube diameter by chemical modifications of an aromatic residue involved in a single close contact

Abstract

Supramolecular self-assembly is an attractive pathway for bottomup synthesis of novel nanomaterials. In particular, this approach allows the spontaneous formation of structures of well-defined shapes and monodisperse characteristic sizes. Because nanotechnology mainly relies on size-dependent physical phenomena, the control of monodispersity is required, but the possibility of tuning the size is also essential. For self-assembling systems, shape, size, and monodispersity are mainly settled by the chemical structure of the building block. Attempts to change the size notably by chemical modification usually end up with the loss of self-assembly. Here, we generated a library of 17 peptides forming nanotubes of monodisperse diameter ranging from 10 to 36 nm. A structural model taking into account close contacts explains how a modification of a few Å of a single aromatic residue induces a fourfold increase in nanotube diameter. The application of such a strategy is demonstrated by the formation of silica nanotubes of various diameters.size control | mineralization | structural approach | size prediction

Physics and engineering of peptide supramolecular nanostructures

“…The cycloalkane ring of this kind of peptides ensures that the peptide backbone has a similar flat 2-D conformation required for the stacking of the cyclic peptide rings. 15 Tarabout et al 31 used the lanreotide octapeptide cyclized peptide scaffold (NH-D-2-Nal-cyclo-[Cys-Tyr-D-Trp-Lys-Val-Cys]-Thr-CONH 2 ) to form nanotubes. It was shown that the inner diameter of the hollow peptide nanotubes can be altered by aromatic residues in a wide range of diameters, from 10 to 36 nm.…”

The development of Army relevant peptide-based surface enhanced Raman scattering (SERS) sensors for biological threat detection

“…The biopanning process typically involves four main steps: preparation of the phage displayed peptide libraries, capture of specific phage that binds to the target, washing of low affinity or non specific phages from the cell surface, and then finally recovery through elution of the enriched target binders for the next round of selection. [74][75][76][77] Using these types of selection techniques, it has been possible to identify and select several different material specific binding peptide sequences (examples include metal compounds, semiconductor materials, minerals, and polymers) 72 as well as particular targets (chemical [78][79][80][81] , biological 65,[82][83] , or energetic hazards [84][85][86][87][88] ). The screening and selection of such phage displayed target binding peptides has attracted particular interest in the research areas of nanotechnology and sensor design.…”

Self-rolled nanotubes with controlled hollow interiors by patterned grafts

“…Therefore, hollow secondary types of architecture including organic microtubes 1 and nanotubes (such as graphene 2 and carbon nanotubes 3 ) have been studied experimentally [1][2][3][4][5][6][7][8][9][10][11] and theoretically. Therefore, hollow secondary types of architecture including organic microtubes 1 and nanotubes (such as graphene 2 and carbon nanotubes 3 ) have been studied experimentally [1][2][3][4][5][6][7][8][9][10][11] and theoretically.…”