title: Stimuli-responsive polypeptide vesicles by conformation-specific assembly.
abstract: In biology, lipids are well known for their ability to assemble into spherical vesicles. Proteins, in particular virus capsids, can also form regular vesicle-like structures, where the precise folding and stable conformations of many identical subunits directs their self-assembly. Functionality present on these subunits also controls their disassembly within the cellular environment, for example, in response to a pH change. Here, we report the preparation of diblock copolypeptides that self-assemble into spherical vesicular assemblies whose size and structure are dictated primarily by the ordered conformations of the polymer segments, in a manner similar to viral capsid assembly. Furthermore, functionality was incorporated into these molecules to render them susceptible to environmental stimuli, which is desirable for drug-delivery applications. The control of assembly and function exhibited in these systems is a significant advance towards the synthesis of materials that can mimic the precise three-dimensional assembly found in proteins.
authors.affiliation: Department of Materials, University of California, Santa Barbara, California 93106, USA.
authors.forename: Enrico G
authors.initials: EG
authors.lastname: Bellomo
authors.forename: Michael D
authors.initials: MD
authors.lastname: Wyrsta
authors.forename: Lisa
authors.initials: L
authors.lastname: Pakstis
authors.forename: Darrin J
authors.initials: DJ
authors.lastname: Pochan
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Deming
mesh_terms: D006863:Hydrogen-Ion Concentration; D008055:Lipids / Q000737:chemistry; D008956:Models, Chemical; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013237:Stereoisomerism
chemical_list: D008055:Lipids; D010455:Peptides; D011108:Polymers