Rhodes D.I.,Avexa Ltd |
Rhodes D.I.,JDJ Bioservices Ltd |
Peat T.S.,CSIRO |
Vandegraaff N.,Avexa Ltd |
And 8 more authors.
ChemBioChem | Year: 2011
An optimised method of solution cyclisation gave us access to a series of peptides including SLKIDNLD (2). We investigated the crystallographic complexes of the HIV integrase (HIV-IN) catalytic core domain with 13 of the peptides and identified multiple interactions at the binding site, including hydrogen bonds with residues Thr125 and Gln95, that have not previously been described as being accessible within the binding site. We show that the peptides inhibit the interaction of lens epithelium-derived growth factor (LEDGF) with HIV-IN in a proximity AlphaScreen assay and in an assay for the LEDGF enhancement of HIV-IN strand transfer. The interactions identified represent a potential framework for the development of new HIV-IN inhibitors. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Ede N.J.,Mimotopes Pty Ltd. |
Hill J.,Agency for Science, Technology and Research Singapore |
Joy J.K.,Agency for Science, Technology and Research Singapore |
Ede A.-M.,Mimotopes Pty Ltd. |
Koppens M.L.,Mimotopes Pty Ltd.
Journal of Peptide Science | Year: 2012
Murray Valley encephalitis virus is a member of the flavivirus group, a large family of single-stranded RNA viruses, which cause serious disease in all regions of the world. Unfortunately, no suitable antivirals are available, and there are commercial vaccines for only three flaviviruses. The solid-phase synthesis of a library of 400 C-terminal arginine peptide aldehydes and their screening against Murray Valley encephalitis virus protease are demonstrated. The library was utilised to elucidate several tripeptide sequences that can be used as inhibitors in further SAR studies. © 2012 European Peptide Society and John Wiley & Sons, Ltd.