title: Functional self-assembling polypeptide bionanomaterials.
abstract: Bionanotechnology seeks to modify and design new biopolymers and their applications and uses biological systems as cell factories for the production of nanomaterials. Molecular self-assembly as the main organizing principle of biological systems is also the driving force for the assembly of artificial bionanomaterials. Protein domains and peptides are particularly attractive as building blocks because of their ability to form complex three-dimensional assemblies from a combination of at least two oligomerization domains that have the oligomerization state of at least two and three respectively. In the present paper, we review the application of polypeptide-based material for the formation of material with nanometre-scale pores that can be used for the separation. Use of antiparallel coiled-coil dimerization domains introduces the possibility of modulation of pore size and chemical properties. Assembly or disassembly of bionanomaterials can be regulated by an external signal as demonstrated by the coumermycin-induced dimerization of the gyrase B domain which triggers the formation of polypeptide assembly.
authors: Department of Biotechnology, National Institute of Chemistry, Ljubljana, Slovenia.
authors: Tibor
authors: T
authors: Doles
authors: Sabina
authors: S
authors: Božič
authors: Helena
authors: H
authors: Gradišar
authors: Roman
authors: R
authors: Jerala
mesh_terms: D049933:Aminocoumarins / Q000494:pharmacology; D001672:Biocompatible Materials / Q000737:chemistry*; D027081:DNA Gyrase / Q000378:metabolism*; D049329:Nanostructures / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D010455:Peptides / Q000737:chemistry*; D055503:Protein Multimerization / Q000187:drug effects
chemical_list: D049933:Aminocoumarins; D001672:Biocompatible Materials; D010455:Peptides; D027081:DNA Gyrase; C004628:coumermycin