Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials
The coiled coil is a superhelical protein structural motif that consists of two or more alpha-helical peptides that are wrapped around each other in superhelical fashion. Coiled coils are amongst the most ubiquitous folding motifs found in proteins and have not only been identified in structural proteins but also play an important role in various intracellular regulation processes as well as membrane fusion. The aim of this critical review is to highlight the potential of coiled coil peptide sequences for the development of self-assembled, responsive and/or bioactive materials. After a short historical overview outlining the discovery of this protein folding motif, the article will briefly discuss naturally occurring coiled coils. After that, the basic rules, which have been established to date for the design of coiled coils will be briefly summarized followed by a presentation of several classes of coiled coils, which may represent interesting candidates for the development of novel self-assembled, responsive and/or bioactive materials. This critical review will end with a section that summarizes the different coiled coil based (hybrid) materials that have been reported to date and which hopefully will help to stimulate further work to explore the full potential of this unique class of protein folding motifs for the development of novel self-assembled, responsive and/or bioactive materials (212 references).
Keywords: De-Novo Design ; Amino-Acid-Sequence ; Heterodimeric Leucine-Zipper ; Peptide-Porphyrin Complexes ; Surface-Plasmon Resonance ; Hybrid Block-Copolymers ; 4-Helix Bundle Protein ; Alpha-Helical Bundle ; Crystal-Structure ; Chain-Length
Record created on 2010-10-07, modified on 2016-08-08