Here We Go Again!

Well, it's been about 12 hours, and the internet 'done blown up' over allegations of plagiarism between a 2013 Chem. Eur.J. and a 2009 JACS. Now, let's say that all this blog coverage brings a lot of otherwise-unwanted attention to your group, and people start to notice other similarities...

...such as the ones between a 2012 Dalton Trans. (same gentleman) and a 2010 JACS, this time from Chuan He's group over at the University of Chicago. Holding these up face-to-face, there sure are a bunch of similarities (again!).

He (p. 2): "In this study an Amt1-based copper(I) fluorescent reporter, Amt1-FRET, was constructed by subcloning the copper-binding domain of Amt1 (residues 36-110) between a cyan fluorescent protein (CFP) and a yellow fluorescent protein (YFP), taking advantage of the copper(I)-binding-induced conformational change of Amt1 (Figure 1b). This strategy, pioneered by Tsien and co-workers, produces a genetically encoded fluorescent reporter by inserting a sensing domain, which undergoes a conformational change upon target binding, between two fluorescent proteins that are fluorescence resonance energy transfer (FRET) pairs.10,11,21 Amt1-FRET was expressed in E. coli in the presence of 1.4 mM CuSO4 and purified to yield the copper(I)-bound Amt1-FRET (Amt1-FRET-Cu) (Figure S2, Supporting Information). The fluorescence spectra of both copper(I)-bound and apo-Amt1-FRET were taken by exciting the FRET donor CFP (433 nm) and recording the fluorescence intensities of the YFP (527 nm) and CFP (477 nm) emissions. An increase in FRET between YFP and CFP in Amt1-FRET in the presence of Cu+ was observed through the increase of the peak ratios (I527/I477) from 1.95 to 2.26 as soon as metal was added (Figure 1c), supporting the proposed copper(I)-binding-induced conformational change of Amt1"

Yan (p. 2): "In this paper a PMtb-based copper(I) fluorescent reporter, PMtb-FRET, was constructed by subcloning the copper(I)- binding domain of Mtb CDC 1551 (residues 1–162) between cyan fluorescent protein (CFP) and yellow fluorescent protein (YFP), taking advantage of the copper(I)-binding induced conformation change of PMtb (Fig. 1) to determine the free concentration of the copper(I) in Mtb protein. This strategy, pioneered by Tsien and coworkers,31 33 produced a genetically encoded fluorescent reporter by inserting a sensing protein domain, which went through a conformational change upon target binding, between two fluorescent proteins that were FRET (fluorescence resonance energy transfer) pairs.31–34 PMtb-FRET was expressed in E. coli in the presence of 1.5 mM CuSO4 and purified to yield the copper(I)-bound PMtb-FRET (PMtb-FRET-Cu) (Fig. S2, ESI†). The fluorescence spectra of both PMtb-FRET-Cu and PMtb- FRET without copper(I) were taken by exciting the FRET donor CFP (433 nm) and recording the fluorescence intensities of the YFP (527 nm) and CFP (477 nm) emissions. An increase in FRET between YFP and CFP in PMtb-FRET in the presence of Cu(I) was observed through the increase of the peak ratios (I527/I477) from 2.01 to 2.45, supporting the proposed copper(I)- binding induced the conformational change of PMtb-FRET (Fig. 1)."

Or how about this swatch?

He (p. 2): "To further investigate if different metal ions interfere with the Cu+ binding, the copper(I)-binding-induced FRET changes were measured in the presence of an equal amount of other metal ions. First, the signal for other metal ions after the addition of 5 equiv of metal to Amt1-FRET was measured, followed by the addition of an equal amount of Cu+ (Figure 2b). In all cases, 100% of the signal was recovered, showing that Cu+ binding is tighter compared to that of other metal ions tested and that the presence of other metal ions does not interfere with copper(I) binding to Amt1-FRET. Also, common anions were shown not to interfere with copper(I) binding"

Yan (p. 3): "To further investigate whether different metal ions would interfere with the Cu(I) binding, the copper(I)-binding-induced FRET changes were measured in the presence of an equal amount of othermetal ions. Firstly, the signal for other metal ions after the addition of 5 equiv ofmetal to PMtb-FRET was measured, followed by the addition of an equal amount of Cu(I) (Fig. 5). In all cases, 100% of the signal was recovered, showing that Cu(I) binding was tighter compared to that of other metal ions tested and that the presence of other metal ions does not interfere with copper(I) binding..."

*Even worse? This time, the forgers couldn't even manage a citation!

I didn't have time today to cantrill the whole thing, but look forward to a lively (continuing!) debate in the Comments. Thanks again to Shawn at WPI for alerting me to the later papers.

Update (1/23/13) - Thanks also to Prof. Chris Goldsmith for the initial hat-tip on this round!