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Issue 20, 2011
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Controlling assembly of helical polypeptidesvia PEGylation strategies

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Abstract

Recent studies in our laboratories have demonstrated that a helical polypeptide (17H6), equipped with a histidine tag and a helical alanine-rich, glutamic-acid-containing domain, exhibits pH-responsive assembly behavior useful in the production of polymorphological nanostructures. In this study, the histidine tag in these polypeptides was replaced by polyethylene glycol (PEG) with different molecular masses (5 kDa, or 10 kDa), and the self-association behavior of 17H6 and the PEGylated conjugates was characterized viadynamic light scattering (DLS), small angle neutron scattering (SANS), and cryogenic transmission electron microscopy (cryo-TEM). DLS experiments illustrated that the polypeptide and its PEG-conjugates undergo reversible assembly under acidic conditions, suggesting that the aggregation state of the polypeptide and the conjugates is controlled by the charged state of the glutamic acid residues. Nanoscale aggregates were detected at polypeptide/conjugate concentrations as low as 20 μM (∼0.3–0.5 mg ml−1) at physiological and ambient temperatures. Scattering and microscopy results showed that the size, the aggregation number, and the morphology of the aggregates can be tuned by the size and the nature of the hydrophilic tag. This tunable nature of the morphology of the aggregates, along with their low critical aggregation concentration, suggests that PEG-alanine-rich polypeptide conjugates may be useful as drug delivery vehicles in which the alanine-rich block serves as a drug attachment domain.

Graphical abstract: Controlling assembly of helical polypeptidesvia PEGylation strategies

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Supplementary files

Article information


Submitted
17 Apr 2011
Accepted
28 Jul 2011
First published
30 Aug 2011

Soft Matter, 2011,7, 9758-9766
Article type
Paper

Controlling assembly of helical polypeptidesvia PEGylation strategies

A. Top, S. Zhong, C. Yan, C. J. Roberts, D. J. Pochan and K. L. Kiick, Soft Matter, 2011, 7, 9758
DOI: 10.1039/C1SM05686G

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