20 July 2014
I am writing with reference to the recent paper by Coskuner and Murray . I am sorry but I find it very hard to believe that these authors were not aware of our previous research in the field of ATP and amyloid-β (Aβ) [2-4]. In this research, we show unequivocally that ATP, ATP + Mg, and ATP +Al (III) (as well as equivalent preparations using ADP and AMP) influence significantly the propensity for Aβ25-35, Aβ1-40, Aβ1-42, and amylin (IAPP) to form β sheets of amyloid under near physiological conditions. May I suggest that the authors’ claimed novelty of their findings is somewhat diminished in the light of our previous (and novel) research in this field.
Christopher Exley, PhD
Professor in Bioinorganic Chemistry
Honorary Professor, University of the Highlands and Islands
 Coskuner O, Murray IV (2014) Adenosine triphosphate (ATP) reduces amyloid-β protein misfolding in vitro. J Alzheimers Dis 41, 561-574.
 Exley C, Birchall JD (1996) Biological availability of aluminium in commercial ATP. J Inorg Biochem 63, 241-252.
 Exley C (1999) A molecular mechanism of aluminium-induced Alzheimer's disease? J Inorg Biochem 76, 133-140.
 Exley C, Korchazhkina O (2001) Promotion of formation of amyloid fibrils by aluminium adenosine triphosphate (AlATP). J Inorg Biochem 84, 215-224.