Cation-pi interactions: Difference between revisions
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| Cation-pi interaction. Surfaces colored by electrostatic potential. Image adapted from one kindly provided by [http://www.its.caltech.edu/~dadgrp/research/molrec/index.html Dennis Dougherty]. | | Cation-pi interaction. Surfaces colored by electrostatic potential. Image adapted from one kindly provided by [http://www.its.caltech.edu/~dadgrp/research/molrec/index.html Dennis Dougherty]. | ||
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Cationic moieties that are within 6.0 Å of the face of an aromatic ring (phenylalanine, tyrosine, or tryptophan) may engage in polar interactions called cation-pi interactions (cation-π interactions). | Cationic moieties that are within 6.0 Å of the face of an aromatic ring (phenylalanine, tyrosine, or tryptophan) may engage in polar interactions called cation-pi interactions (cation-π interactions)<ref name="GD" /><ref name="dad2013">PMID: 23214924</ref><ref name="dad2025">PMID: 39977669</ref>. | ||
The flat face of an aromatic ring has a partial negative charge owing to the [[#Chemistry|pi electrons]]. <!-- ([http://www.molphys.leidenuniv.nl/monos/smo/index.html?basics/photophysics.htm schematic], [http://www.webelements.com/shop/product.php/129/molyorbital_molecular_orbital_organic_structures_set physical model]). --> | The flat face of an aromatic ring has a partial negative charge owing to the delocalized [[#Chemistry|pi electrons]]. <!-- ([http://www.molphys.leidenuniv.nl/monos/smo/index.html?basics/photophysics.htm schematic], [http://www.webelements.com/shop/product.php/129/molyorbital_molecular_orbital_organic_structures_set physical model]). --> | ||
Cations such as the sidechains of Lys or Arg, cationic ligands, or metal cations often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref name='GD'>PMID: 10449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. Gallivan and Dougherty (1999)<ref name='GD' /> concluded that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". They can also contribute significantly to intermolecular contacts and interactions with ligands. | Cations such as the sidechains of Lys or Arg, cationic ligands, or metal cations often align themselves centered over the faces of aromatic rings. Over one fourth of Trp's in the Protein Data Bank interact with cations, and 99% of significant cation-pi interactions occur within a distance of 6.0 Angstroms <ref name='GD'>PMID: 10449714</ref>. Cation-pi interactions make a significant contribution to the overall stability of most proteins. Gallivan and Dougherty (1999)<ref name='GD' /> concluded that "cation-pi interactions should be considered alongside the more conventional hydrogen bonds, salt bridges, and hydrophobic effects in any analysis of protein structure". They can also contribute significantly to intermolecular contacts and interactions with ligands. | ||
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==Examples== | ==Examples== | ||
<StructureSection load='1gai' size='350' side='right' scene='Cation-pi_interactions/Nicotine_catpi/5' caption='Cation-pi interactions'> | |||
===Nicotinic Acetylcholine Receptor and Nicotine Addiction=== | ===Nicotinic Acetylcholine Receptor and Nicotine Addiction=== | ||
====Receptor==== | ====Receptor==== | ||
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====Cation-Pi Interactions==== | ====Cation-Pi Interactions==== | ||
In 1998, Zhong ''et al.'' (with Dougherty)<ref name="zhong">PMID: 9770444</ref> provided evidence that the [http://en.wikipedia.org/wiki/Nicotinic_acetylcholine_receptor cation in '''acetylcholine'''] engages in a cation-pi interaction with Trp149 in the '''neuronal-type''' receptor, making an important contribution to the binding affinity. In 2002, Beene ''et al.'' (with Dougherty)<ref name="beene">PMID: 12162741</ref> provided evidence that no such cation-pi interaction is involved when '''nicotine''' binds to the '''muscle-type''' receptor, thus accounting in part for the lower affinity. In 2009, Xiu ''et al.'' (with Dougherty)<ref name="XD" /> provided evidence that a strong cation-pi interaction occurs between the cation of '''nicotine''' and Trp149 in the '''neuronal-type''' receptor. The lower affinity of nicotine for the muscle-type, compared to the neuronal type receptors, is accounted for by differences in cation-pi interaction strength and the absence of a nicotine-receptor hydrogen bond in the former<ref name="XD" />. | In 1998, Zhong ''et al.'' (with Dougherty)<ref name="zhong">PMID: 9770444</ref> provided evidence that the [http://en.wikipedia.org/wiki/Nicotinic_acetylcholine_receptor cation in '''acetylcholine'''] engages in a cation-pi interaction with Trp149 in the '''neuronal-type''' receptor, making an important contribution to the binding affinity. In 2002, Beene ''et al.'' (with Dougherty)<ref name="beene">PMID: 12162741</ref> provided evidence that no such cation-pi interaction is involved when '''nicotine''' binds to the '''muscle-type''' receptor, thus accounting in part for the lower affinity. In 2009, Xiu ''et al.'' (with Dougherty)<ref name="XD" /> provided evidence that a strong cation-pi interaction occurs between the cation of '''nicotine''' and Trp149 in the '''neuronal-type''' receptor. The lower affinity of nicotine for the muscle-type, compared to the neuronal type receptors, is accounted for by differences in cation-pi interaction strength and the absence of a nicotine-receptor hydrogen bond in the former<ref name="XD" />. | ||
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*[[:Category:Cation_pi|Entries in Proteopedia's Cation pi Category]] (no hyphen) | *[[:Category:Cation_pi|Entries in Proteopedia's Cation pi Category]] (no hyphen) | ||
*[[:Category:Cation-pi_interaction|Entries in Proteopedia's Cation-pi interaction Category]] | *[[:Category:Cation-pi_interaction|Entries in Proteopedia's Cation-pi interaction Category]] | ||
</StructureSection> | |||
==Literature References & Notes== | ==Literature References & Notes== | ||
<references/> | <references/> | ||
