| Literature DB >> 15034560 |
Enrico G Bellomo1, Michael D Wyrsta, Lisa Pakstis, Darrin J Pochan, Timothy J Deming.
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.Entities:
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Year: 2004 PMID: 15034560 DOI: 10.1038/nmat1093
Source DB: PubMed Journal: Nat Mater ISSN: 1476-1122 Impact factor: 43.841