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Conformational and aggregation properties of a PEGylated alanine-rich polypeptide.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Top, Ayben Roberts, Christopher J. Kiick, Kristi L. |
| Copyright Year | 2011 |
| 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. |
| File Format | PDF HTM / HTML |
| PubMed reference number | 21553871 |
| Journal | Medline |
| Volume Number | 12 |
| Issue Number | 6 |
| Alternate Webpage(s) | http://openaccess.iyte.edu.tr/bitstream/handle/11147/5062/5062.pdf?isAllowed=y&sequence=1 |
| Alternate Webpage(s) | https://doi.org/10.1021/bm200272w |
| Journal | Biomacromolecules |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
