Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 506664
Title Nanoparticle-Templated Formation and Growth Mechanism of Curved Protein Polymer Fibrils
Author(s) Pham, Thao T.H.; Rombouts, Wolf H.; Fokkink, Remco; Stuart, Marc C.A.; Cohen Stuart, Martien A.; Kleijn, Mieke
Source Biomacromolecules 17 (2016)7. - ISSN 1525-7797 - p. 2392 - 2398.
DOI http://dx.doi.org/10.1021/acs.biomac.6b00486
Department(s) Physical Chemistry and Soft Matter
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2016
Abstract

We investigated the growth of biosynthetic protein polymers with templated curvature 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. Because 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 nanocapsules from designed protein polymers

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