Nanoparticle-templated formation and growth mechanism of curved protein polymer fibrils

Thao T.H. Pham, Wolf Harald Rombouts, Remco G. Fokkink, Marc C.A. Stuart, Martien A. Cohen Stuart, J. Mieke Kleijn

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Abstract

We investigated templated fibril growth of biosynthetic protein polymers on pluronic nanospheres. The protein has a central silk-like block containing glutamic residues (SE) and collagen-like end-blocks (C). The SE blocks stack into filaments when their charge is removed (pH < 5). Indeed, at low pH curved and circular fibers are formed at the surface of the nanospheres, which keep their shape after removal of the pluronics. The data reveal the mechanism of the templated fibril-growth: the growth of protein assemblies is nucleated in solution; small protein fibrils adsorb on the nanospheres, presumably due to hydrogen bond formation between the silk-like blocks and the pluronic PEO blocks; the surface of the pluronic particles templates further growth. At relatively low protein/pluronic weight ratios, only a fraction of the nanospheres bears protein fibers, pointing to a limiting amount of nuclei in solution. Since the nanospheres capture fibrils at an early stage of growth, they can be used to separate growth and nucleation rates in protein fibril formation. Moreover, the nanoparticle-templated growth of stable curved fibers opens ways to build proteinaceous nano-capsules from designed protein polymers.

Original languageEnglish
Pages (from-to)2392-2398
Number of pages7
JournalBiomacromolecules
Volume17
Issue number7
DOIs
Publication statusPublished - 11-Jul-2016

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