Abstract:In nature, biological nanomaterials are synthesized under ambient conditions in a natural microscopic‐sized laboratory, such as a cell. Biological molecules, such as peptides and proteins, undergo self‐assembly processes in vivo and in vitro, and these monomers are assembled into various nanometer‐scale structures at room temperature and atmospheric pressure. The self‐assembled peptide nanostructures can be further organized to form nanowires, nanotubes, and nanoparticles via their molecular‐recognition functi… Show more
“…In this regard S. Banta et al in 2007 researched about engineering of protein and peptide building blocks for nanotechnology usage [7] and the interactions that lead to the formation of these structures include chiral dipole-dipole interactions, π-π stacking, hydrogen bonds, nonspecific Van der Waals interactions, hydrophobic forces, electrostatic interactions, and repulsive steric forces [8]. Biological molecules such as peptides and proteins undergo self-assembly processes in vivo and in vitro, and these monomers are assembled into various nanometer-scale structures at room temperatures and atmospheric pressure [9]. The self-assembled protein and peptide nanostructures can be further organized to form various nanowires, nanotubes, and nanoparticles via their molecular-recognition functions.…”
New water-based nanofluids including unparalleled milk protein α-lactalbumin hollow nano-bio-tubes using low cost, available and advanced partial chemical hydrolysis strategy in bottom-up nano-assembly have been employed in this work. The aqueous sol-gel chemistry in nanotechnology which we selected for this goal offers new fabrication as interesting smart protein nanotubes. The kinds of nanometer sized tubular structures such as waved, helically coiled, bent, bamboo-shaped, bead-like and branched single-walled protein nanotubes (SWPNTs) with a range of 3 -8 nm in outer diameters were produced by this method. Complete characterization for natural produced nanotubes including SEM, TEM images, G bond and D bond in Raman spectroscopy, XRD patterns, DLS (Dynamic Light Scattering) and FTIR analysis were evaluated which they are most significant experiments in synthesized protein nanotubes soluble in clear water nanofluids and stabilization of transparent nanofluids was proved within more than one year after preparation. Various necessary ligand ion salts such as Mn 2+ , Zn 2+ and Ca 2+ or mixtures as bridge makers and producing biological self-assembly hollow SWPNTs were performed and we focused on new chemical technology under specific acidic hydrolysis method not conventional enzymatic proteolysis and applying surfactants, pH reagent, Tris-HCl buffer, polar solvent which could be produced by β-sheet stacked hydrolysed protein α-lactalbumin mechanism under appropriate conditions to achieving high efficiency new protein nanotubes skeleton. They can be promising materials applied in food science, diet nutrition, nanomedicine, nano-biotechnology and surgery.
“…In this regard S. Banta et al in 2007 researched about engineering of protein and peptide building blocks for nanotechnology usage [7] and the interactions that lead to the formation of these structures include chiral dipole-dipole interactions, π-π stacking, hydrogen bonds, nonspecific Van der Waals interactions, hydrophobic forces, electrostatic interactions, and repulsive steric forces [8]. Biological molecules such as peptides and proteins undergo self-assembly processes in vivo and in vitro, and these monomers are assembled into various nanometer-scale structures at room temperatures and atmospheric pressure [9]. The self-assembled protein and peptide nanostructures can be further organized to form various nanowires, nanotubes, and nanoparticles via their molecular-recognition functions.…”
New water-based nanofluids including unparalleled milk protein α-lactalbumin hollow nano-bio-tubes using low cost, available and advanced partial chemical hydrolysis strategy in bottom-up nano-assembly have been employed in this work. The aqueous sol-gel chemistry in nanotechnology which we selected for this goal offers new fabrication as interesting smart protein nanotubes. The kinds of nanometer sized tubular structures such as waved, helically coiled, bent, bamboo-shaped, bead-like and branched single-walled protein nanotubes (SWPNTs) with a range of 3 -8 nm in outer diameters were produced by this method. Complete characterization for natural produced nanotubes including SEM, TEM images, G bond and D bond in Raman spectroscopy, XRD patterns, DLS (Dynamic Light Scattering) and FTIR analysis were evaluated which they are most significant experiments in synthesized protein nanotubes soluble in clear water nanofluids and stabilization of transparent nanofluids was proved within more than one year after preparation. Various necessary ligand ion salts such as Mn 2+ , Zn 2+ and Ca 2+ or mixtures as bridge makers and producing biological self-assembly hollow SWPNTs were performed and we focused on new chemical technology under specific acidic hydrolysis method not conventional enzymatic proteolysis and applying surfactants, pH reagent, Tris-HCl buffer, polar solvent which could be produced by β-sheet stacked hydrolysed protein α-lactalbumin mechanism under appropriate conditions to achieving high efficiency new protein nanotubes skeleton. They can be promising materials applied in food science, diet nutrition, nanomedicine, nano-biotechnology and surgery.
“…Nanowires grown on biomolecular templates received attention since the recognition functions of these biomolecules with specific ligands can be tuned to wire molecular electronic devices with desired geometries. [1][2][3] Most of the biomolecular-nanowire templates from DNAs or peptides need to be fabricated for them to function in a suitable electric device, and there is an extensive effort to coat them with metals and semiconductors. [4][5][6][7][8][9][10][11] While these biomolecular-nanowire templates appear to be promising building blocks for nanodevices, it is essential to have size monodispersity, rigidness, and product yield to impact the real world.…”
“…Self-assembled peptide-based nanotubes have gained broad attention because of their high biocompatibility and the extraordinary ability to control their properties through modications introduced to the monomeric unit. 22 Although small linear peptides [23][24][25] and even protein fragments extracted from natural motifs [26][27][28][29][30] (e.g. le-handed b-helices) can be also used as organizer units of pepide-based nanotubes (Fig.…”
The structure and stability of the nanotube obtained by assembling peptidepolymer conjugates consisting of two poly(n-butyl acrylate) blocks coupled tohave been investigated at the molecular level using atomistic molecular dynamics simulations. The effect of the wrapping polymer shells in the tube-like core, which consists of stacked b-sheet cyclopeptides, has been examined by simulating assemblies of both unsubstituted cyclopeptides, and conjugates in chloroform and N,N-dimethylformamide solutions. Furthermore, the influence of the environment has been investigated by comparing conjugate assemblies in solution with those deposited on mica. In addition, nanotubes stabilized by b-sheet-like hydrogen bonds between both parallel and antiparallel oriented cyclopeptides have been considered in all cases. The results, which have been analysed in terms of energy contributions, partial radial distribution functions, inter-subunit distances, shape of the cyclopeptide ring, internal van der Waals diameters, and both height and width of the nanostructures deposited on mica, have provided important microscopic insights. For example, analysis of both the energy terms and the structural dynamics obtained for the different assemblies indicate that the mica surface interacts more favourably with the parallel assembly than with the antiparallel ones, whereas the only configuration that is structurally stable in solution is the latter. Furthermore, adsorption onto the solid substrate produces a small deformation of the cylindrical molecular system.
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