Fluorescence quenching to study protein-ligand binding: common errors.
A number of recent articles, amongst others several published in the Journal of Fluorescence, use inappropriate fluorescence methodology to determine ligand binding characteristics to (mostly) proteins. In this Letter, several common pitfalls are discussed in relation to two recent publications in the Journal of Fluorescence (Wang et al. (2009) 19:801-808; Ding et al. (2009) 19:783-791). The Author hopes that this contribution helps to prevent a further spread of the incorrect methodology, and results in a reappraisal of those articles already published using similar methodology.
van de Weert
Marco
M
Department of Pharmaceutics and Analytical Chemistry, Faculty of Pharmaceutical Sciences, University of Copenhagen, Universitetsparken 2, DK-2100 Copenhagen, Denmark. mvdw@farma.ku.dk
D000465:Algorithms; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D008024:Ligands; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012815:Signal Processing, Computer-Assisted; D013050:Spectrometry, Fluorescence / Q000379:methods*
D008024:Ligands; D011506:Proteins