In this section
Anaesthesia makes up the largest hospital speciality and has a huge role to play in nearly every aspect of any hospital from operating theatres to accident and emergency, to the labour ward, and to intensive care. Our research ranges from basic molecular research into mechanisms of anaesthesia to investigating the clinical impact of novel anaesthetic agents.
Our research covers the entirety of patient’s perioperative journey and through this, we aim to deliver the greatest impact. The section has been pioneering in the development of novel technologies to facilitate the delivery of anaesthetic agents and has also made pivotal in-roads into the mechanism of action of anaesthetic agents and their wider application to other diseases (such as their protective roles in brain injury and in cancer).
@article{Bertaccini:2014:10.1021/cn500172e,
author = {Bertaccini, EJ and Dickinson, R and Trudell, JR and Franks, NP},
doi = {10.1021/cn500172e},
journal = {ACS Chemical Neuroscience},
pages = {1246--1252},
title = {Molecular modeling of a tandem two pore domain potassium channel reveals a putative binding Site for general anesthetics},
url = {http://dx.doi.org/10.1021/cn500172e},
volume = {5},
year = {2014}
}
TY - JOUR
AB - Anesthetics are thought to mediate a portion of their activity via binding to and modulation of potassium channels. In particular, tandem pore potassium channels (K2P) are transmembrane ion channels whose current is modulated by the presence of general anesthetics and whose genetic absence has been shown to confer a level of anesthetic resistance. While the exact molecular structure of all K2P forms remains unknown, significant progress has been made toward understanding their structure and interactions with anesthetics via the methods of molecular modeling, coupled with the recently released higher resolution structures of homologous potassium channels to act as templates. Such models reveal the convergence of amino acid regions that are known to modulate anesthetic activity onto a common three- dimensional cavity that forms a putative anesthetic binding site. The model successfully predicts additional important residues that are also involved in the putative binding site as validated by the results of suggested experimental mutations. Such a model can now be used to further predict other amino acid residues that may be intimately involved in the target-based structure–activity relationships that are necessary for anesthetic binding.
AU - Bertaccini,EJ
AU - Dickinson,R
AU - Trudell,JR
AU - Franks,NP
DO - 10.1021/cn500172e
EP - 1252
PY - 2014///
SN - 1948-7193
SP - 1246
TI - Molecular modeling of a tandem two pore domain potassium channel reveals a putative binding Site for general anesthetics
T2 - ACS Chemical Neuroscience
UR - http://dx.doi.org/10.1021/cn500172e
UR - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000346682000014&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR - http://hdl.handle.net/10044/1/32932
VL - 5
ER -