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Chemical biology

More charges against aggregation

Nature volume 449, page 555 (2007)Cite this article

Protein aggregation causes problems for biotechnology and leads to many fatal human diseases. But a grasp of the physical principles involved enables 'superproteins' to be designed that have exceptional solubilities.

Proteins evolved under the stringent conditions imposed by the cellular environment. This means that, out of the vast number of possible amino-acid sequences in proteins, only a tiny fraction actually occur in nature. The advent of protein engineering1 provides an opportunity to create proteins that have sequences that have never been found in living organisms, and that could have properties unparalleled in their natural counterparts. Reporting in the Journal of the American Chemical Society, Liu and colleagues2 show that it is possible to design functional proteins with very high electrostatic charge that turn out to be far more soluble in water than their naturally occurring analogues.

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Figure 1: An exploration chart of protein amino-acid sequences.

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Authors and Affiliations

  1. Michele Vendruscolo and Christopher M. Dobson are in the Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.,

    Michele Vendruscolo & Christopher M. Dobson

Authors
  1. Michele Vendruscolo
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  2. Christopher M. Dobson
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Vendruscolo, M., Dobson, C. More charges against aggregation. Nature 449, 555 (2007). https://doi.org/10.1038/449555a

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