TDP‐43 as structure‐based biomarker in amyotrophic lateral sclerosis
Léon Beyer, René Günther, Jan Christoph Koch, Stephan Klebe, Tim Hagenacker, Paul Lingor, Anne‐Sophie Biesalski, Andreas Hermann, Andreas Nabers, Ralf Gold, Lars Tönges, Klaus Gerwert
Abstract
Pathologic alterations of Transactivation response DNA-binding protein 43 kilo Dalton (TDP-43) are a major hallmark of amyotrophic lateral sclerosis (ALS). In this pilot study, we analyzed the secondary structure distribution of TDP-43 in cerebrospinal fluid of ALS patients (n = 36) compared to Parkinson´s disease patients (PD; n = 30) and further controls (Ctrl; n = 24) using the immuno-infrared sensor technology. ALS patients could be discriminated from PD and Ctrl with a sensitivity/specificity of 89 %/77 % and 89 %/83 %, respectively. Our findings demonstrate that TDP-43 misfolding measured by the immuno-infrared sensor technology has the potential to serve as a biomarker candidate for ALS.