Please use this identifier to cite or link to this item:
https://hdl.handle.net/11147/5062
Title: | Conformational and aggregation properties of a pegylated alanine-rich polypeptide | Authors: | Top, Ayben Roberts, Christopher J. Kiick, Kristi L. |
Keywords: | Acidic conditions Sheet formation Elevated temperature Polypeptides Amino acids |
Publisher: | American Chemical Society | Source: | Top, A., Roberts, C.J., and Kiick, K.L. (2011). Conformational and aggregation properties of a pegylated alanine-rich polypeptide. Biomacromolecules, 12(6), 2184-2192. doi:10.1021/bm200272w | Abstract: | The conformational and aggregation behavior of PEG conjugates of an alanine-rich polypeptide (PEG-c17H6) were investigated and compared to that of the polypeptide equipped with a deca-histidine tag (17H6). These polypeptides serve as simple and stimuli-responsive models for the aggregation behavior of helix-rich proteins, as our previous studies have shown that the helical 17H6 self-associates at acidic pH and converts to β-sheet structures at elevated temperature under acidic conditions. In the work here, we show that PEG-c17H6 also adopts a helical structure at ambient/subambient temperatures, at both neutral and acidic pH. The thermal denaturation behavior of 17H6 and PEG-c17H6 is similar at neutral pH, where the alanine-rich domain has no self-association tendency. At acidic pH and elevated temperature, however, PEGylation slows β-sheet formation of c17H6, and reduces the apparent cooperativity of thermally induced unfolding. Transmission electron microscopy of PEG-c17H6 conjugates incubated at elevated temperatures showed fibrils with widths of ∼20-30 nm, wider than those observed for fibrils of 17H6. These results suggest that PEGylation reduces β-sheet aggregation in these polypeptides by interfering, only after unfolding of the native helical structure, with interprotein conformational changes needed to form β-sheet aggregates. | URI: | https://doi.org/10.1021/bm200272w http://hdl.handle.net/11147/5062 |
ISSN: | 1526-4602 1525-7797 |
Appears in Collections: | Chemical Engineering / Kimya Mühendisliği PubMed İndeksli Yayınlar Koleksiyonu / PubMed Indexed Publications Collection Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection WoS İndeksli Yayınlar Koleksiyonu / WoS Indexed Publications Collection |
Show full item record
CORE Recommender
SCOPUSTM
Citations
24
checked on Nov 29, 2024
WEB OF SCIENCETM
Citations
25
checked on Nov 9, 2024
Page view(s)
880
checked on Dec 2, 2024
Download(s)
890
checked on Dec 2, 2024
Google ScholarTM
Check
Altmetric
Items in GCRIS Repository are protected by copyright, with all rights reserved, unless otherwise indicated.