Refolding protein aggregates

See allHide authors and affiliations

Science  22 Apr 2016:
Vol. 352, Issue 6284, pp. 425-426
DOI: 10.1126/science.352.6284.425-g

Although protein chaperones direct the correct folding of nascent proteins, they also can resolubilize protein aggregates that may have formed to enable their refolding. Polymers such as poly(ethylene glycol) can help keep proteins in their native state by preventing thermal denaturation and aggregation. Nakamoto et al. now report that acrylamide polymer nanoparticles (80 to 160 nm in diameter), with anioic and hydrophobic groups that can solubilize aggregates of lysozyme, allow it to refold into its native configuration. Like chaperones, these nanoparticles appear to have a high affinity for the aggregate state but only weak affinity for the native one.

J. Am. Chem. Soc. 10.1021/jacs.5b12600 (2016).

Navigate This Article