By Aitziber L. Cortajarena, Tijana Z. Grove
This booklet is dedicated to the engineering of protein-based nanostructures and nanomaterials. One key problem in nanobiotechnology is in order to make the most the normal repertoire of protein buildings and services to construct fabrics with outlined homes on the nanoscale utilizing “bottom-up” suggestions. This ebook addresses in an built-in demeanour the entire serious features that must be understood and regarded to layout the following iteration of nano-bio assemblies. The e-book covers first the basics of the layout and lines of the protein development blocks and their self-assembly illustrating probably the most correct examples of nanostructural layout. eventually, the ebook features a part devoted to proven purposes of those novel bioinspired nanostructures in numerous fields from hybrid nanomaterials to regenerative medication. This booklet offers a accomplished up to date assessment of this quickly evolving field.
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Extra info for Protein-based Engineered Nanostructures
Haines LA, Rajagopal K, Ozbas B et al (2005) Light- activated hydrogel formation via the triggered folding and self-assembly of a designed peptide. J Am Chem Soc 127:17025–17029. Yanlian Y, Ulung K, Xiumei W et al (2009) Designer self-assembling peptide nanomaterials. Nano Today 4:193–210. Saaem I, LaBean TH (2013) Overview of DNA origami for molecular self-assembly. WIREs Nanomed Nanobiotechnol 5:150–162. Walshaw J, Woolfson DN (2001) SOCKET: a program for identifying and analysing coiled-coil motifs within protein structures.
This measurement is consistent with the authors’ proposed model for metal-promoted radial assembly (Fig. 6). The bipyridine ligands of three adjacent triple helices formed two metal-ion coordination sites; the addition of Fe(II) promoted radial assembly of triple helices and creation of peptide discs . To extend upon this work, Chmielewski et al. modified the design of H-(byp)2 to incorporate an additional bipyridine ligand with the goal of inducing disc assembly in the absence of metal ions .
Under acidic conditions without salt, the peptide exhibited a net positive charge. Salt addition decreased the electrostatic repulsion between fibrils allowing for twisting and in the case of higher salt concentrations closing of the twisted fibrils into nanotubes . Numerous studies of fibrillogenic β-sheet peptides have indicated significant polymorphism, in which different self-assembled forms, including fibrils, coiled ribbons, and tubes, in a manner that depended on the solution conditions under which the peptides were assembled .
Protein-based Engineered Nanostructures by Aitziber L. Cortajarena, Tijana Z. Grove