Artificial Polymers Mimic Bacteriophage Capsid Proteins To Protect and Functionalize Nucleic Acid Structures

摘要

The filamentous bacteriophage ml3 and related viruses encapsulate DNA with protein, forming an organic nanowire about 1 micrometer long and less then 10 nanometers wide. The length of the wire is formed from many copies of a single protein, which is a single alpha helix formed from about 50 amino acids. It can be viewed as a very sophisticated surfactant, with hydrophilic regions that interact with the DNA and form the outer surface, and hydrophobic regions that pack against each other. We have implemented these design principles in peptoids (sequence-specific N-functional glycine oligomers) and have found that they form aggregates with DNA that have adjustable properties. This approach may complement phage display methods, providing new approaches to gene transfection and nanofabrication that do not require expression in bacteria and that provide a wider range of chemical stability and functionality.