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 489970
Title The supramolecular organization of a peptide-based nanocarrier at high molecular detail
Author(s) Rad-Malekshahi, M.; Visscher, K.M.; Rodrigues, J.P.G.L.M.; Vries, R.J. de; Hennink, W.E.; Baldus, M.; Bonvin, A.M.J.J.; Mastrobattista, E.
Source Journal of the American Chemical Society 137 (2015)24. - ISSN 0002-7863 - p. 7775 - 7784.
DOI https://doi.org/10.1021/jacs.5b02919
Department(s) Physical Chemistry and Soft Matter
VLAG
Publication type Refereed Article in a scientific journal
Publication year 2015
Keyword(s) solid-state nmr - protein secondary structure - chemical-shift index - force-field - polypeptide vesicles - drug-delivery - beta-sheet - dynamics - nanovesicles - spectroscopy
Abstract Nanovesicles self-assembled from amphiphilic peptides are promising candidates for applications in drug delivery. However, complete high-resolution data on the local and supramolecular organization of such materials has been elusive thus far, which is a substantial obstacle to their rational design. In the absence of precise information, nanovesicles built of amphiphilic “lipid-like” peptides are generally assumed to resemble liposomes that are organized from bilayers of peptides with a tail-to-tail ordering. Using the nanocarrier formed by the amphiphilic self-assembling peptide 2 (SA2 peptide) as an example, we derive the local and global organization of a multimega-Dalton peptide-based nanocarrier at high molecular detail and at close-to physiological conditions. By integrating a multitude of experimental techniques (solid-state NMR, AFM, SLS, DLS, FT-IR, CD) with large- and multiscale MD simulations, we show that SA2 nanocarriers are built of interdigitated antiparallel ß-sheets, which bear little resemblance to phospholipid liposomes. Our atomic level study allows analyzing the vesicle surface structure and dynamics as well as the intermolecular forces between peptides, providing a number of potential leads to improve and tune the biophysical properties of the nanocarrier. The herein presented approach may be of general utility to investigate peptide-based nanomaterials at high-resolution and at physiological conditions.
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