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A dehydron is an intramolecular hydrogen bond incompletely shielded from water attack, with a propensity to promote its own dehydration. Dehydrons constitute a special kind of packing defect in soluble proteins and were named and characterized by Argentine-born American scientist Ariel Fernandez, from Rice University, and his coworkers Ridgway Scott, Stephen Berry and Harold Scheraga.
Additional recommended knowledge
Dehydrons are partially dehydrated amide-carbonyl hydrogen bonds that result from an incomplete clustering of side-chain nonpolar groups that "wrap" the polar pair within the protein structure. Dehydrons are sticky, since they promote the removal of surrounding water through protein associations and/or ligand binding. This further dehydration enhances the electrostatic interaction between the amide and carbonyl groups by de-shielding their partial charges. Furthermore, the dehydration stabilizes the hydrogen bond by destabilizing the nonbonded state that consists of dehydrated isolated charges. Hence, the name dehydron makes reference to the tendency to promote its dehydration, a process both energetically and thermodynamically favored. Thus, dehydrons are markers for protein interactivity, and hence functional indicators, and may possibly serve as drug targets.
Dehydron patterns are not conserved across paralog proteins, hence dehydrons constitute structural singularities that may be targeted by drug ligands to achieve higher specificity and ultimately, to curb side effects. This observation prompted Ariel Fernandez to introduce the design concept of "drug as dehydron wrapper", and heralded the advent of a novel approach to drug development based on the so-called wrapping technology.
Dehydrons in the news:
Re-engineered gleevec curbs heart-related complications:
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Dehydron". A list of authors is available in Wikipedia.|