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Issue 11, 2008
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Protein wrapping: a molecular marker for association, aggregation and drug design

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Abstract

In this tutorial review we survey the concept of protein wrapping from a physico-chemical perspective. Wrapping is introduced as an indicator of the packing quality of protein structure. Thus, while a well-wrapped protein is sustainable in isolation, a poorly wrapped protein is reliant on binding partnerships to maintain its structural integrity. At a local level, wrapping is indicative of the extent of solvent exposure of the amidecarbonyl hydrogen bonds of the protein backbone. Poorly wrapped hydrogen bonds, the so-called dehydrons, are shown to represent structural vulnerabilities. These singularities are sticky, hence promoters of protein associations. We also focus on severely under-wrapped protein structures that belong to an order/disorder twilight. Such proteins are shown to be prone to aggregate. Finally, we survey the recent exploitation of dehydrons as targetable features to promote specificity in drug-based cancer therapy. Dehydrons prove to be valuable targets to reduce side effects and enhance drug safety.

Graphical abstract: Protein wrapping: a molecular marker for association, aggregation and drug design

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Article information


Submitted
26 Jun 2008
First published
15 Sep 2008

Chem. Soc. Rev., 2008,37, 2373-2382
Article type
Tutorial Review

Protein wrapping: a molecular marker for association, aggregation and drug design

A. Fernández and A. Crespo, Chem. Soc. Rev., 2008, 37, 2373
DOI: 10.1039/B804150B

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