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Title: Controlling assembly of helical polypeptides via PEGylation strategies
Authors: Top, Ayben
Zhong, Sheng
Yan, Congqi
Roberts, Christopher J.
Pochan, Darrin J.
Kiick, Kristi L.
Keywords: Aggregation state
Charged state
Cryogenic transmission electron microscopy
Drug delivery systems
Issue Date: 21-Oct-2011
Publisher: Royal Society of Chemistry
Source: Top, A., Zhong, S., Yan, C., Roberts, C.J., Pochan, D.J.,and Kiick, K.L. (2011). Controlling assembly of helical polypeptides via PEGylation strategies. Soft Matter, 7(20). 9758-9766. doi:10.1039/c1sm05686g
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 via dynamic 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.
ISSN: 1744-683X
Appears in Collections:Chemical Engineering / Kimya Mühendisliği
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection

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