Abstract
Protein aggregation and protein self-assembly is an important occurrence in natural systems, and is in some form or other dictated by biopolymers. Very obvious influences of biopolymers on protein assemblies are, e.g., virus particles. Viruses are a multi-protein assembly of which the morphology is dictated by poly-nucleotides namely RNA or DNA. This “biopolymer” directs the proteins and imposes limitations on the structure like the length or diameter of the particle. Not only do these bionanoparticles use polymer-directed self-assembly, also processes like amyloid formation are in a way a result of directed protein assembly by partial unfolded/misfolded biopolymers namely, polypeptides. The combination of proteins and synthetic polymers, inspired by the natural processes, are therefore regarded as a highly promising area of research. Directed protein assembly is versatile with respect to the possible interactions which brings together the protein and polymer, e.g., electrostatic, v.d. Waals forces or covalent conjugation, and possible combinations are numerous due to the large amounts of different polymers and proteins available. The protein-polymer interacting behavior and overall morphology is envisioned to aid in clarifying protein-protein interactions and are thought to entail some interesting new functions and properties which will ultimately lead to novel bio-hybrid materials.
Highlights
IntroductionSelf-association and -assembly is a key factor for it to function. Whether it is phospholipids forming the membranes of cells and organelles, proteins assembled within the lipid bilayer for regulating trans-membrane transport, polynucleotides like RNA in combination with proteins forming the ribosomes or the microtubules which are built from a protein dimer aggregating up to 20–25 μm in length with a width of only 25 nm, and provide strength to the cell and act as an intra-cellular highway along which transport occurs
In nature, self-association and -assembly is a key factor for it to function
The controlled assembly of the viral coat proteins around the natural RNA-sequence can be used to target, e.g., surfaces, when the RNA is attached by one side to a planar or particle surface, the same directed protein assembly can be used to structure the surface with coat proteins
Summary
Self-association and -assembly is a key factor for it to function. Whether it is phospholipids forming the membranes of cells and organelles, proteins assembled within the lipid bilayer for regulating trans-membrane transport, polynucleotides like RNA in combination with proteins forming the ribosomes or the microtubules which are built from a protein dimer aggregating up to 20–25 μm in length with a width of only 25 nm, and provide strength to the cell and act as an intra-cellular highway along which transport occurs. Many of the processes are dictated by polymeric species (oligo- and polypeptides/polynucleotides) and it is important to highlight the progress made in synthetic polymer induced and polymer directed protein assembly with respect to the development of new systems and approaches. Possible is a combination of the two approaches, while some proteins would not display any affinity for certain polymers or oligomers, when modified with a small molecular component or receptor, specific and direct assembly can be induced which combines very well with many supramolecular polymeric hydrogel systems [13] In such coordinated systems, charge interactions with specific metal ligand residues is possible, and hydrophobic interactions or hydrogen-bonding can be used (Figure 1b). The mentioned approaches will be addressed according to the most recently performed studies and system developments
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