Calixar and Aston University together in collaborative research to tackle multidrug resistance targets
Posted: 21 October 2014 | Calixar
Aston University (Birmingham – UK) and Calixar SAS (Lyon-France) have concluded a new research agreement through the “BBSRC Industrial CASE Studentship Competition 2013” framework…
Aston University (Birmingham – UK) and Calixar SAS (Lyon-France) have concluded a new research agreement through the “BBSRC Industrial CASE Studentship Competition 2013” framework. The annual CASE competition for collaborative training awards provides students with a first-rate research training experience, allowing top quality bioscience graduates to undertake research, leading to a PhD.
The purpose of Calixar’s collaborative project with Aston is to study the extraction, stabilization and crystallization of full-length human ABC transporters involved in multidrug resistance.
“I am delighted to be able to use Calixar technology to investigate the structural features of this important protein family,” said Dr Alice ROTHNIE, who has worked on ABC transporters for over ten years and is the Principal Investigator on the project. “The partnership between Aston and Calixar will allow us to increase our understanding of the structure and function of these very important proteins building on the unique stabilizing properties of Calixar molecules” said co-investigator Professor Roslyn BILL.
“We are very pleased to strengthen our collaboration with Aston University” said Dr Anass Jawhari, CSO. “Calixar will provide proprietary processes for the native and functional isolation of targets and their crystallization. This common effort aims to investigate structure/function relationships and the molecular basis of multidrug resistance proteins to find new leads and to derive conformational antibodies”.
This project will also demonstrate the added value of innovative processes and technologies set up by partners for structural based drug discovery applications of challenging human targets of high medical relevance. This work will provide molecular and mechanistic insights into multidrug resistance and pave the way to work with other membrane protein targets that are intractable to structural investigation.