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dc.contributor.authorTop, Ayben
dc.contributor.authorZhong, Sheng
dc.contributor.authorYan, Congqi
dc.contributor.authorRoberts, Christopher J.
dc.contributor.authorPochan, Darrin J.
dc.contributor.authorKiick, Kristi L.
dc.date.accessioned2017-03-01T11:30:52Z
dc.date.available2017-03-01T11:30:52Z
dc.date.issued2011-10-21
dc.identifier.citationTop, 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/c1sm05686gen_US
dc.identifier.issn1744-683X
dc.identifier.urihttp://doi.org/10.1039/c1sm05686g
dc.identifier.urihttp://hdl.handle.net/11147/4936
dc.description.abstractRecent 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.en_US
dc.description.sponsorshipNational Institutes of Health (NIH); National Center for Research Resources (NCRR) (1-P20-RR017716; 1-RO1-EB006006; P30-RR031160; National Aeronautics and Space Administration (NA68-01923); Center for Neutron Science at University of Delaware (70NANB7H6178)en_US
dc.language.isoengen_US
dc.publisherRoyal Society of Chemistryen_US
dc.relation.isversionof10.1039/c1sm05686gen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectAggregation stateen_US
dc.subjectCharged stateen_US
dc.subjectPEgylationen_US
dc.subjectPolypeptidesen_US
dc.subjectCryogenic transmission electron microscopyen_US
dc.subjectDrug delivery systemsen_US
dc.titleControlling assembly of helical polypeptides via PEGylation strategiesen_US
dc.typearticleen_US
dc.contributor.authorIDTR114274en_US
dc.contributor.iztechauthorTop, Ayben
dc.relation.journalSoft Matteren_US
dc.contributor.departmentİYTE, Mühendislik Fakültesi, Kimya Mühendisliği Bölümüen_US
dc.identifier.volume7en_US
dc.identifier.issue20en_US
dc.identifier.startpage9758en_US
dc.identifier.endpage9766en_US
dc.identifier.wosWOS:000295582000028
dc.identifier.scopusSCOPUS:2-s2.0-80053611637
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US


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