Department of Drug Design and Pharmacology > Employees
Nanda Gowtham Aduri
2100 København Ø
Bioavailability of a drug is dependent on its ability to cross the lipid layer of the cellular membranes. This poses a major hurdle in the design of new drugs, and a very large percentage of drug trials fail due to limited membrane permeability. The idea of using transport proteins, located in the membrane, as vehicles of drug uptake has emerged during the past 15 years, as it was found that several orally distributed drugs were being transported by intestinal transporters. Optimal use of such proteins as drug uptake vehicles requires a thorough understanding of their biochemistry and knowledge of the three-dimensional structure and the molecular mechanism associated with the transport process. The proton driven peptide transporter hPepT1 is one of the most important drug transporters in the small intestine as several drugs have been shown to be hPepT1 substrates. The total commercial values of the drugs taken up daily in 2010 by hPepT1 were more than one billion US dollars. A detailed study in this field would provide an excellent platform for novel drug design of compounds with enhanced bioavailability. Considering the complications in studying a human membrane protein, in this project we will use the bacterial peptide transporter YjdL as a model system.
Critical role of a conserved transmembrane lysine in substrate recognition by the proton-coupled oligopeptide transporter YjdLJensen, J. M., Aduri, N. G., Prabhala, B. K., Jahnsen, R., Franzyk, H. & Mirza, O. A. 24 Sep 2014 In : International Journal of Biochemistry & Cell Biology. 55, p. 311-17 7 p.
Publication: Research - peer-review › Journal article