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Self-assembling cages from coiled-coil peptide modules.

ABSTRACT: An ability to mimic the boundaries of biological compartments would improve our understanding of self-assembly and provide routes to new materials for the delivery of drugs and biologicals and the development of protocells. We show that short designed peptides can be combined to form unilamellar spheres approximately 100 nanometers in diameter. The design comprises two, noncovalent, heterodimeric and homotrimeric coiled-coil bundles. These are joined back to back to render two complementary hubs, which when mixed form hexagonal networks that close to form cages. This design strategy offers control over chemistry, self-assembly, reversibility, and size of such particles.

SUBMITTER: Fletcher JM

PROVIDER: S-EPMC6485442 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature

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Self-assembling cages from coiled-coil peptide modules.

Fletcher Jordan M JM Harniman Robert L RL Barnes Frederick R H FR Boyle Aimee L AL Collins Andrew A Mantell Judith J Sharp Thomas H TH Antognozzi Massimo M Booth Paula J PJ Linden Noah N Miles Mervyn J MJ Sessions Richard B RB Verkade Paul P Woolfson Derek N DN

Science (New York, N.Y.) 20130411 6132

An ability to mimic the boundaries of biological compartments would improve our understanding of self-assembly and provide routes to new materials for the delivery of drugs and biologicals and the development of protocells. We show that short designed peptides can be combined to form unilamellar spheres approximately 100 nanometers in diameter. The design comprises two, noncovalent, heterodimeric and homotrimeric coiled-coil bundles. These are joined back to back to render two complementary hubs ...[more]

PMID: 23579496

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